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Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers

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Inorganic Chemistry 2014, 53 (22) , 11925-11936. https://doi.org/10.1021/ic5011677Ambika Bhagi-Damodaran, Igor D. Petrik, Nicholas M. Marshall, Howard Robinson, and Yi Lu . Systematic Tuning of Heme Redox Potentials and Its Effects on O2 Reduction Rates in a Designed Oxidase in Myoglobin. Journal of the American Chemical Society 2014, 136 (34) , 11882-11885. https://doi.org/10.1021/ja5054863Isabella Daidone, Licia Paltrinieri, Andrea Amadei, Gianantonio Battistuzzi, Marco Sola, Marco Borsari, and Carlo Augusto Bortolotti . Unambiguous Assignment of Reduction Potentials in Diheme Cytochromes. The Journal of Physical Chemistry B 2014, 118 (27) , 7554-7560. https://doi.org/10.1021/jp506017aLucyano J. A. Macedo, Ayaz Hassan, Graziela C. Sedenho, Frank N. Crespilho. Assessing electron transfer reactions and catalysis in multicopper oxidases with operando X-ray absorption spectroscopy. 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Coordination Chemistry Reviews 2020, 416 , 213335. https://doi.org/10.1016/j.ccr.2020.213335Narsis Attar, Oscar A. Campos, Maria Vogelauer, Chen Cheng, Yong Xue, Stefan Schmollinger, Lukasz Salwinski, Nathan V. Mallipeddi, Brandon A. Boone, Linda Yen, Sichen Yang, Shannon Zikovich, Jade Dardine, Michael F. Carey, Sabeeha S. Merchant, Siavash K. Kurdistani. The histone H3-H4 tetramer is a copper reductase enzyme. Science 2020, 369 (6499) , 59-64. https://doi.org/10.1126/science.aba8740Valiallah Hosseininasab, Alison C. McQuilken, Abolghasem (Gus) Bakhoda, Jeffery A. Bertke, Qadir K. Timerghazin, Timothy H. Warren. Lewis Acid Coordination Redirects S‐Nitrosothiol Signaling Output. Angewandte Chemie 2020, 132 (27) , 10946-10950. https://doi.org/10.1002/ange.202001450Valiallah Hosseininasab, Alison C. McQuilken, Abolghasem (Gus) Bakhoda, Jeffery A. Bertke, Qadir K. Timerghazin, Timothy H. Warren. Lewis Acid Coordination Redirects S‐Nitrosothiol Signaling Output. Angewandte Chemie International Edition 2020, 59 (27) , 10854-10858. https://doi.org/10.1002/anie.202001450Jonathan Szuster, Ulises A. Zitare, María A. Castro, Alcides J. Leguto, Marcos N. Morgada, Alejandro J. Vila, Daniel H. Murgida. Cu A -based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential. Chemical Science 2020, 11 (24) , 6193-6201. https://doi.org/10.1039/D0SC01620ABrian R. Lydon, Chi Chung Lee, Kazuki Tanifuji, Nathaniel S. Sickerman, Megan P. Newcomb, Yilin Hu, Markus W. Ribbe, Jenny Y. Yang. Electrochemical Characterization of Isolated Nitrogenase Cofactors from Azotobacter vinelandii. ChemBioChem 2020, 21 (12) , 1773-1778. https://doi.org/10.1002/cbic.201900425Si-min Tang, Ze-hao Xu, Ya-lei Liu, Guang-feng Yang, Jun Mu, Ren-cun Jin, Qiao Yang, Xiao-ling Zhang. Performance, kinetics characteristics and enhancement mechanisms in anammox process under Fe(II) enhanced conditions. Biodegradation 2020, 170 https://doi.org/10.1007/s10532-020-09905-yMotahareh Motalebi, Hamid Golchoubian, Ehsan Rezaee. Structural and chromotropism properties of copper(II) complexes containing a tridentate ligand. Chemical Papers 2020, 39 https://doi.org/10.1007/s11696-020-01228-9Jaime M. Murphy, Brian A. Powell, Julia L. Brumaghim. Stability constants of bio-relevant, redox-active metals with amino acids: The challenges of weakly binding ligands. Coordination Chemistry Reviews 2020, 412 , 213253. https://doi.org/10.1016/j.ccr.2020.213253S. Maria, Taraknath Chattopadhyay, S. Ananya, Subrata Kundu. Reduction of nitrite to NO at a mononuclear copper(II)-phenolate site. Inorganica Chimica Acta 2020, 506 , 119515. https://doi.org/10.1016/j.ica.2020.119515Wenyu Gu, Ross D. Milton. Natural and Engineered Electron Transfer of Nitrogenase. Chemistry 2020, 2 (2) , 322-346. https://doi.org/10.3390/chemistry2020021Wei Liu, Shuping Zhang, Sergei Nekhai, Sijin Liu. Depriving Iron Supply to the Virus Represents a Promising Adjuvant Therapeutic Against Viral Survival. Current Clinical Microbiology Reports 2020, 7 (2) , 13-19. https://doi.org/10.1007/s40588-020-00140-wRoghayeh Jafarpour, Faezeh Fatemi, Akram Eidi, Faramarz Mehrnejad. Effect of the Met148Leu Mutation on the Structure and Dynamics of the Rusticyanin Protein from Acidithiobacillus sp. FJ2. Journal of Biomolecular Structure and Dynamics 2020, , 1-19. https://doi.org/10.1080/07391102.2020.1775119Diego Plaza-Lozano, Daniel Morales-Martínez, Felipe J. González, Juan Olguín. Homoleptic Mononuclear Tris-Chelate Complexes of Fe II , Co II , Ni II , and Zn II Based on a Redox-Active Imidazolyl-2-thione Ligand: Structural and Electrochemical Correlation. European Journal of Inorganic Chemistry 2020, 2020 (17) , 1562-1573. https://doi.org/10.1002/ejic.202000120Ulises A. Zitare, Jonathan Szuster, María C. Santalla, Marcos N. Morgada, Alejandro J. Vila, Daniel H. Murgida. Dynamical effects in metalloprotein heterogeneous electron transfer. Electrochimica Acta 2020, 342 , 136095. https://doi.org/10.1016/j.electacta.2020.136095Karim Zuhra, Fiona Augsburger, Tomas Majtan, Csaba Szabo. Cystathionine-β-synthase: Molecular Regulation and Pharmacological Inhibition. Biomolecules 2020, 10 (5) , 697. https://doi.org/10.3390/biom10050697Gordana Gajić, Lola Djurdjević, Olga Kostić, Snežana Jarić, Branka Stevanović, Miroslava Mitrović, Pavle Pavlović. Phytoremediation Potential, Photosynthetic and Antioxidant Response to Arsenic-Induced Stress of Dactylis glomerata L. Sown on Fly Ash Deposits. Plants 2020, 9 (5) , 657. https://doi.org/10.3390/plants9050657Marcus J. Edwards, David J. Richardson, Catarina M. Paquete, Thomas A. Clarke. Role of multiheme cytochromes involved in extracellular anaerobic respiration in bacteria. Protein Science 2020, 29 (4) , 830-842. https://doi.org/10.1002/pro.3787M.S. Yusseppone, V.A. Bianchi, J.M. Castro, T. Noya Abad, Y.S. Minaberry, S.E. Sabatini, C.M. Luquet, M.C. Rios de Molina, I. Rocchetta. In situ experiment to evaluate biochemical responses in the freshwater mussel Diplodon chilensis under anthropogenic eutrophication conditions. Ecotoxicology and Environmental Safety 2020, 193 , 110341. https://doi.org/10.1016/j.ecoenv.2020.110341Alfonso Schiavi, Flavie Strappazzon, Natascia Ventura. Mitophagy and iron: two actors sharing the stage in age-associated neuronal pathologies. Mechanisms of Ageing and Development 2020, , 111252. https://doi.org/10.1016/j.mad.2020.111252Masaru Kato, Ichizo Yagi. Electrocatalytic Oxygen Reduction at Multinuclear Metal Active Sites Inspired by Metalloenzymes. e-Journal of Surface Science and Nanotechnology 2020, 18 (0) , 81-93. https://doi.org/10.1380/ejssnt.2020.81Tyler B. J. Pinter, Karl J. Koebke, Vincent L. Pecoraro. Katalyse und Elektronentransfer in helikalen De‐novo‐Gerüststrukturen. Angewandte Chemie 2020, 256 https://doi.org/10.1002/ange.201907502Tyler B. J. Pinter, Karl J. Koebke, Vincent L. Pecoraro. Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds. Angewandte Chemie International Edition 2020, 460 https://doi.org/10.1002/anie.201907502Jin Li, Yajun Zheng, Jia Zhao, Daniel E. Austin, Zhiping Zhang. Matrix-assisted nanoelectrospray mass spectrometry for soft ionization of metal( i )–protein complexes. The Analyst 2020, 145 (5) , 1646-1656. https://doi.org/10.1039/C9AN02117ECuiping Zhao, Zhe Lyu, Feng Long, Taiwo Akinyemi, Kasidet Manakongtreecheep, Dieter Söll, William B. Whitman, David J. Vinyard, Yuchen Liu. The Nbp35/ApbC homolog acts as a nonessential [4Fe‐4S] transfer protein in methanogenic archaea. FEBS Letters 2020, 594 (5) , 924-932. https://doi.org/10.1002/1873-3468.13673Bingyan Wu, Joshua T. Atkinson, Dimithree Kahanda, George N. Bennett, Jonathan J. Silberg. Combinatorial design of chemical‐dependent protein switches for controlling intracellular electron transfer. AIChE Journal 2020, 66 (3) https://doi.org/10.1002/aic.16796Hui Wang, Hui Shi, Malini Rajan, Elizabeth R. Canarie, Seoyeon Hong, Daniele Simoneschi, Michele Pagano, Matthew F. Bush, Stefan Stoll, Elizabeth A. Leibold, Ning Zheng. FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster. Molecular Cell 2020, https://doi.org/10.1016/j.molcel.2020.02.011Adrian Ruff, Felipe Conzuelo, Wolfgang Schuhmann. Bioelectrocatalysis as the basis for the design of enzyme-based biofuel cells and semi-artificial biophotoelectrodes. Nature Catalysis 2020, 3 (3) , 214-224. https://doi.org/10.1038/s41929-019-0381-9Ying-Wu Lin. Uranyl Binding to Proteins and Structural-Functional Impacts. Biomolecules 2020, 10 (3) , 457. https://doi.org/10.3390/biom10030457Kartik S. Aiyer. How does electron transfer occur in microbial fuel cells?. World Journal of Microbiology and Biotechnology 2020, 36 (2) https://doi.org/10.1007/s11274-020-2801-zWeixing Deng, Pengfei Sun, Quli Fan, Lei Zhang, Tsuyoshi Minami. Highly selective detection of copper(II) by a “ligand-free” conjugated copolymer in nucleophilic solvents. Frontiers of Chemical Science and Engineering 2020, 14 (1) , 105-111. https://doi.org/10.1007/s11705-019-1791-6Soraia Meghdadi, Niloofar Khodaverdian, Azadeh Amirnasr, Pim J. French, Martin E. van Royen, Erik A.C. Wiemer, Mehdi Amirnasr. A new carboxamide probe as On-Off fluorescent and colorimetric sensor for Fe3+ and application in detecting intracellular Fe3+ ion in living cells. Journal of Photochemistry and Photobiology A: Chemistry 2020, 389 , 112193. https://doi.org/10.1016/j.jphotochem.2019.112193Hubert Müller, Sviatlana Marozava, Alexander J. Probst, Rainer U. Meckenstock. Groundwater cable bacteria conserve energy by sulfur disproportionation. The ISME Journal 2020, 14 (2) , 623-634. https://doi.org/10.1038/s41396-019-0554-1Marcos N. Morgada, María-Eugenia Llases, Estefanía Giannini, María-Ana Castro, Pedro M. Alzari, Daniel H. Murgida, María-Natalia Lisa, Alejandro J. Vila. Unexpected electron spin density on the axial methionine ligand in Cu A suggests its involvement in electron pathways. Chemical Communications 2020, 56 (8) , 1223-1226. https://doi.org/10.1039/C9CC08883KJeffrey J. Warren, Harry B. Gray. Electron Transfer Proteins. 2020,,https://doi.org/10.1016/B978-0-12-409547-2.14831-0Biraj Das, Manash J. Baruah, Mukesh Sharma, Bipul Sarma, Galla V. Karunakar, Lanka Satyanarayana, Subhasish Roy, Pradip K. Bhattacharyya, Kamala Kanta Borah, Kusum K. Bania. Self pH regulated iron(II) catalyst for radical free oxidation of benzyl alcohols. Applied Catalysis A: General 2020, 589 , 117292. https://doi.org/10.1016/j.apcata.2019.117292Santosh L. Saraf, Victor R. Gordeuk. Iron. 2020,,, 83-102. https://doi.org/10.1016/B978-0-12-805378-2.00006-1Flavia Nastri, Daniele D’Alonzo, Linda Leone, Gerardo Zambrano, Vincenzo Pavone, Angela Lombardi. Engineering Metalloprotein Functions in Designed and Native Scaffolds. Trends in Biochemical Sciences 2019, 44 (12) , 1022-1040. https://doi.org/10.1016/j.tibs.2019.06.006Yibing Deng, Tao Wu, Mengdi Wang, Shengchao Shi, Guodong Yuan, Xi Li, Hanchung Chong, Bin Wu, Peng Zheng. Enzymatic biosynthesis and immobilization of polyprotein verified at the single-molecule level. Nature Communications 2019, 10 (1) https://doi.org/10.1038/s41467-019-10696-xHammed Olawale Oloyede, Joseph Anthony Orighomisan Woods, Helmar Görls, Winfried Plass, Abiodun Omokehinde Eseola. The necessity of free and uncrowded coordination environments in biomimetic complex models: oxidative coupling by mixed-ligand cobalt( ii ) complexes of diazene–disulfonamide. New Journal of Chemistry 2019, 43 (46) , 18322-18330. https://doi.org/10.1039/C9NJ04396AChristina Ferousi, Simon Lindhoud, Frauke Baymann, Eric R. Hester, Joachim Reimann, Boran Kartal. Discovery of a functional, contracted heme-binding motif within a multiheme cytochrome. Journal of Biological Chemistry 2019, 294 (45) , 16953-16965. https://doi.org/10.1074/jbc.RA119.010568Dorian Marckmann, Petru-Iulian Trasnea, Johannes Schimpf, Christine Winterstein, Andreea Andrei, Stefan Schmollinger, Crysten E. Blaby-Haas, Thorsten Friedrich, Fevzi Daldal, Hans-Georg Koch. The cbb3 -type cytochrome oxidase assembly factor CcoG is a widely distributed cupric reductase. Proceedings of the National Academy of Sciences 2019, 116 (42) , 21166-21175. https://doi.org/10.1073/pnas.1913803116E. Altin, S. Altundag, S. Altin, A. Bayri. Fabrication of Cr doped Na0.67Fe0.5Mn0.5O2 compounds and investigation of their structural, electrical, magnetic and electrochemical properties. Journal of Materials Science: Materials in Electronics 2019, 30 (19) , 17848-17855. https://doi.org/10.1007/s10854-019-02136-9Donghui Lu, Bo Xing, Yuhan Liu, Zhirong Wang, Xiangyang Xu, Liang Zhu. Enhanced production of short-chain fatty acids from waste activated sludge by addition of magnetite under suitable alkaline condition. Bioresource Technology 2019, 289 , 121713. https://doi.org/10.1016/j.biortech.2019.121713Dixit Sharma, Ankita Sharma, Birbal Singh, Shailender Kumar Verma. Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic Pathogen Orientia tsutsugamushi. Frontiers in Genetics 2019, 10 https://doi.org/10.3389/fgene.2019.00797David J. Vinyard, Syed Lal Badshah, M. Rita Riggio, Divya Kaur, Annaliesa R. Fanguy, M. R. Gunner. Photosystem II oxygen-evolving complex photoassembly displays an inverse H/D solvent isotope effect under chloride-limiting conditions. Proceedings of the National Academy of Sciences 2019, 116 (38) , 18917-18922. https://doi.org/10.1073/pnas.1910231116Emily R. Featherston, Hannah R. Rose, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, Joseph A. Cotruvo. Biochemical and Structural Characterization of XoxG and XoxJ and Their Roles in Lanthanide‐Dependent Methanol Dehydrogenase Activity. ChemBioChem 2019, 20 (18) , 2360-2372. https://doi.org/10.1002/cbic.201900184Cristina M. Cordas, José J.G. Moura. Molybdenum and tungsten enzymes redox properties – A brief overview. Coordination Chemistry Reviews 2019, 394 , 53-64. https://doi.org/10.1016/j.ccr.2019.05.005Li Huang, Lixing Huang, Lingmin Zhao, Yingxue Qin, Yongquan Su, Qingpi Yan. The regulation of oxidative phosphorylation pathway on Vibrio alginolyticus adhesion under adversities. MicrobiologyOpen 2019, 8 (8) , e00805. https://doi.org/10.1002/mbo3.805B.D. Bennett, J.A. Gralnick. Mechanisms of toxicity by and resistance to ferrous iron in anaerobic systems. Free Radical Biology and Medicine 2019, 140 , 167-171. https://doi.org/10.1016/j.freeradbiomed.2019.06.027Randa Zarban, Malvina Vogler, Aloysius Wong, Joerg Eppinger, Salim Al-Babili, Chris Gehring. Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana. Molecules 2019, 24 (15) , 2691. https://doi.org/10.3390/molecules24152691Ying-Wu Lin. Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters. Molecules 2019, 24 (15) , 2743. https://doi.org/10.3390/molecules24152743Ya Xie, Liqiang Yan, Jianping Li. An On–Off–On Fluorescence Probe Based on Coumarin for Cu 2+ , Cysteine, and Histidine Detections. Applied Spectroscopy 2019, 73 (7) , 794-800. https://doi.org/10.1177/0003702818821329Elizabeth L. Onderko, Daniel A. Phillips, Brian J. Eddie, Matthew D. Yates, Zheng Wang, Leonard M. Tender, Sarah M. Glaven. Electrochemical Characterization of Marinobacter atlanticus Strain CP1 Suggests a Role for Trace Minerals in Electrogenic Activity. Frontiers in Energy Research 2019, 7 https://doi.org/10.3389/fenrg.2019.00060Risnita Vicky Listyarini, Diana Sofia Gesto, Pedro Paiva, Maria João Ramos, Pedro Alexandrino Fernandes. Benchmark of Density Functionals for the Calculation of the Redox Potential of Fe3+/Fe2+ Within Protein Coordination Shells. Frontiers in Chemistry 2019, 7 https://doi.org/10.3389/fchem.2019.00391Rona R. Ramsay. Electron carriers and energy conservation in mitochondrial respiration. ChemTexts 2019, 5 (2) https://doi.org/10.1007/s40828-019-0085-4Byoung-Hoon Lee, Sunghak Park, Minho Kim, Arun K. Sinha, Seong Chan Lee, Euiyeon Jung, Woo Je Chang, Kug-Seung Lee, Jeong Hyun Kim, Sung-Pyo Cho, Hyungjun Kim, Ki Tae Nam, Taeghwan Hyeon. Reversible and cooperative photoactivation of single-atom Cu/TiO2 photocatalysts. Nature Materials 2019, 18 (6) , 620-626. https://doi.org/10.1038/s41563-019-0344-1Rafael Pernil, Enrico Schleiff. Metalloproteins in the Biology of Heterocysts. Life 2019, 9 (2) , 32. https://doi.org/10.3390/life9020032Dao‐Bo Li, Jie Li, Dong‐Feng Liu, Xin Ma, Lei Cheng, Wen‐Wei Li, Chen Qian, Yang Mu, Han‐Qing Yu. Potential regulates metabolism and extracellular respiration of electroactive Geobacter biofilm. Biotechnology and Bioengineering 2019, 116 (5) , 961-971. https://doi.org/10.1002/bit.26928Kamal Zeamari, Guillaume Gerbaud, Sandrine Grosse, Vincent Fourmond, Florence Chaspoul, Frédéric Biaso, Pascal Arnoux, Monique Sabaty, David Pignol, Bruno Guigliarelli, Bénédicte Burlat. Tuning the redox properties of a [4Fe-4S] center to modulate the activity of Mo-bisPGD periplasmic nitrate reductase. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2019, 1860 (5) , 402-413. https://doi.org/10.1016/j.bbabio.2019.01.003Mohit Kumar, Kushneet Kaur Sodhi, Preeti Singh, Pawan Kumar Agrawal, Dileep Kumar Singh. Synthesis and characterization of antibiotic-metal complexes [FeCl3(L1)2H2O and Ni(NO3)2(L2)2H2O] and enhanced antibacterial activity. Environmental Nanotechnology, Monitoring & Management 2019, 11 , 100209. https://doi.org/10.1016/j.enmm.2019.100209Richard Grunzke, Volker Hartmann, Thomas Jejkal, Helen Kollai, Ajinkya Prabhune, Hendrik Herold, Aline Deicke, Christiane Dressler, Julia Dolhoff, Julia Stanek, Alexander Hoffmann, Ralph Müller-Pfefferkorn, Torsten Schrade, Gotthard Meinel, Sonja Herres-Pawlis, Wolfgang E. Nagel. The MASi repository service — Comprehensive, metadata-driven and multi-community research data management. Future Generation Computer Systems 2019, 94 , 879-894. https://doi.org/10.1016/j.future.2017.12.023Helmut Bischof, Sandra Burgstaller, Markus Waldeck-Weiermair, Thomas Rauter, Maximilian Schinagl, Jeta Ramadani-Muja, Wolfgang F. Graier, Roland Malli. Live-Cell Imaging of Physiologically Relevant Metal Ions Using Genetically Encoded FRET-Based Probes. Cells 2019, 8 (5) , 492. https://doi.org/10.3390/cells8050492Jinho Yoon, Taek Lee, Jeong-Woo Choi. Development of Bioelectronic Devices Using Bionanohybrid Materials for Biocomputation System. Micromachines 2019, 10 (5) , 347. https://doi.org/10.3390/mi10050347Michal Wagner, Katrine Qvortrup, Katja E. Grier, Mikkel R. Ottosen, Jonas O. Petersen, David Tanner, Jens Ulstrup, Jingdong Zhang. Gold–carbonyl group interactions in the electrochemistry of anthraquinone thiols self-assembled on Au(111)-surfaces. Chemical Science 2019, 10 (14) , 3927-3936. https://doi.org/10.1039/C9SC00061EM. Akram, A. Dietl, U. Mersdorf, S. Prinz, W. Maalcke, J. Keltjens, C. Ferousi, N. M. de Almeida, J. Reimann, B. Kartal, M. S. M. Jetten, K. Parey, T. R. M. Barends. A 192-heme electron transfer network in the hydrazine dehydrogenase complex. Science Advances 2019, 5 (4) , eaav4310. https://doi.org/10.1126/sciadv.aav4310Meghan A. Smith, Sean H. Majer, Avery C. Vilbert, Kyle M. Lancaster. Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460. Chemical Science 2019, 10 (13) , 3756-3764. https://doi.org/10.1039/C9SC00195FKaren O’Hanlon. Plant Growth-Promoting Bacteria Field Trials in Europe. 2019,,, 371-389. https://doi.org/10.1017/9781108607667.018Maria Angelica D. Rea, Pierre-Alain Wulser, Joël Brugger, Barbara Etschmann, Andrew Bissett, Jeremiah Shuster, Frank Reith. Effect of physical and biogeochemical factors on placer gold transformation in mountainous landscapes of Switzerland. Gondwana Research 2019, 66 , 77-92. https://doi.org/10.1016/j.gr.2018.10.006Hai-Xiao Liu, Lianzhi Li, Xin-Zhi Yang, Chuan-Wan Wei, Hui-Min Cheng, Shu-Qin Gao, Ge-Bo Wen, Ying-Wu Lin. Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin. RSC Advances 2019, 9 (8) , 4172-4179. https://doi.org/10.1039/C8RA10390AAmbika Bhagi-Damodaran, Yi Lu. The Periodic Table’s Impact on Bioinorganic Chemistry and Biology’s Selective Use of Metal Ions. 2019,,, 153-173. https://doi.org/10.1007/430_2019_45Robert Crichton. Basic Coordination Chemistry for Biologists. 2019,,, 19-34. https://doi.org/10.1016/B978-0-12-811741-5.00002-3Gordana Gajić, Miroslava Mitrović, Pavle Pavlović. Ecorestoration of Fly Ash Deposits by Native Plant Species at Thermal Power Stations in Serbia. 2019,,, 113-177. https://doi.org/10.1016/B978-0-12-813912-7.00004-1Ulises A. Zitare, Jonathan Szuster, Magali F. Scocozza, Andrés Espinoza-Cara, Alcides J. Leguto, Marcos N. Morgada, Alejandro J. Vila, Daniel H. Murgida. The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions. Electrochimica Acta 2019, 294 , 117-125. https://doi.org/10.1016/j.electacta.2018.10.069Firoz Shah Tuglak Khan, Amit Kumar, Dipti Lai, Sankar Prasad Rath. Ethene-bridged diiron porphyrin dimer as models of diheme cytochrome c: Structure-function correlation and modulation of heme redox potential. Inorganica Chimica Acta 2019, 484 , 503-512. https://doi.org/10.1016/j.ica.2018.09.047Dan Meyerstein. Reactions of Alkyl Radicals in Aqueous Solutions*. 2018,,, 73-103. https://doi.org/10.1002/9781119379256.ch4Julia Stanek, Marc Konrad, Johannes Mannsperger, Alexander Hoffmann, Sonja Herres-Pawlis. Influence of Functionalized Substituents on the Electron-Transfer Abilities of Copper Guanidinoquinoline Complexes. European Journal of Inorganic Chemistry 2018, 2018 (46) , 4997-5006. https://doi.org/10.1002/ejic.201801078Andrew C. Weitz, Ethan A. Hill, Victoria F. Oswald, Emile L. Bominaar, Andrew S. Borovik, Michael P. Hendrich, Yisong Guo. Probing Hydrogen Bonding Interactions to Iron‐Oxido/Hydroxido Units by 57 Fe Nuclear Resonance Vibrational Spectroscopy. Angewandte Chemie 2018, 130 (49) , 16242-16246. https://doi.org/10.1002/ange.201810227Andrew C. Weitz, Ethan A. Hill, Victoria F. Oswald, Emile L. Bominaar, Andrew S. Borovik, Michael P. Hendrich, Yisong Guo. Probing Hydrogen Bonding Interactions to Iron‐Oxido/Hydroxido Units by 57 Fe Nuclear Resonance Vibrational Spectroscopy. Angewandte Chemie International Edition 2018, 57 (49) , 16010-16014. https://doi.org/10.1002/anie.201810227Grace W Chong, Amruta A Karbelkar, Mohamed Y El-Naggar. Nature’s conductors: what can microbial multi-heme cytochromes teach us about electron transport and biological energy conversion?. Current Opinion in Chemical Biology 2018, 47 , 7-17. https://doi.org/10.1016/j.cbpa.2018.06.007Yasuhiro Ohki, Keisuke Uchida, Mizuki Tada, Roger E. Cramer, Takashi Ogura, Takehiro Ohta. N2 activation on a molybdenum–titanium–sulfur cluster. Nature Communications 2018, 9 (1) https://doi.org/10.1038/s41467-018-05630-6Oriana S. Fisher, Grace E. Kenney, Matthew O. Ross, Soo Y. Ro, Betelehem E. Lemma, Sharon Batelu, Paul M. Thomas, Victoria C. Sosnowski, Caroline J. DeHart, Neil L. Kelleher, Timothy L. Stemmler, Brian M. Hoffman, Amy C. Rosenzweig. Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. Nature Communications 2018, 9 (1) https://doi.org/10.1038/s41467-018-06681-5Xiaohong Liu, Fuying Kang, Cheng Hu, Li Wang, Zhen Xu, Dandan Zheng, Weimin Gong, Yi Lu, Yanhe Ma, Jiangyun Wang. A genetically encoded photosensitizer protein facilitates the rational design of a miniature photocatalytic CO2-reducing enzyme. Nature Chemistry 2018, 10 (12) , 1201-1206. https://doi.org/10.1038/s41557-018-0150-4Pollyana Santos Queiroz, France Anne Dias Ruas, Natália Rocha Barboza, William de Castro Borges, Renata Guerra-Sá. Alterations in the proteomic composition of Serratia marcescens in response to manganese (II). BMC Biotechnology 2018, 18 (1) https://doi.org/10.1186/s12896-018-0493-3Yasuhiro Ohki, Keisuke Uchida, Ryota Hara, Mami Kachi, Mayu Fujisawa, Mizuki Tada, Yoichi Sakai, W. M. C. Sameera. Cubane‐Type [Mo 3 S 4 M] Clusters with First‐Row Groups 4–10 Transition‐Metal Halides Supported by C 5 Me 5 Ligands on Molybdenum. Chemistry – A European Journal 2018, 24 (64) , 17138-17147. https://doi.org/10.1002/chem.201804083Dipti Lai, Firoz Shah Tuglak Khan, Sankar Prasad Rath. Multiheme proteins: effect of heme–heme interactions. Dalton Transactions 2018, 47 (41) , 14388-14401. https://doi.org/10.1039/C8DT00518DMarco Chino, Linda Leone, Gerardo Zambrano, Fabio Pirro, Daniele D'Alonzo, Vincenzo Firpo, Diaa Aref, Liliana Lista, Ornella Maglio, Flavia Nastri, Angela Lombardi. Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages. Biopolymers 2018, 109 (10) , e23107. https://doi.org/10.1002/bip.23107Isman Kurniawan, Kazutomo Kawaguchi, Mitsuo Shoji, Toru Matsui, Yasuteru Shigeta, Hidemi Nagao. A Theoretical Study on Redox Potential and p Ka of [2Fe-2S] Cluster Model from Iron-Sulfur Proteins. Bulletin of the Chemical Society of Japan 2018, 91 (9) , 1451-1456. https://doi.org/10.1246/bcsj.20180116Giorgio Caserta, Marco Chino, Vincenzo Firpo, Gerardo Zambrano, Linda Leone, Daniele D'Alonzo, Flavia Nastri, Ornella Maglio, Vincenzo Pavone, Angela Lombardi. Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design. ChemBioChem 2018, 19 (17) , 1823-1826. https://doi.org/10.1002/cbic.201800200Linda H. Doerrer. Cu in biology: Unleashed by O2 and now irreplaceable. Inorganica Chimica Acta 2018, 481 , 4-24. https://doi.org/10.1016/j.ica.2017.11.051Anja Hemschemeier, Thomas Happe. The plasticity of redox cofactors: from metalloenzymes to redox-active DNA. Nature Reviews Chemistry 2018, 2 (9) , 231-243. https://doi.org/10.1038/s41570-018-0029-3Sebastian Beblawy, Thea Bursac, Catarina Paquete, Ricardo Louro, Thomas A. Clarke, Johannes Gescher. Extracellular reduction of solid electron acceptors by Shewanella oneidensis. Molecular Microbiology 2018, 109 (5) , 571-583. https://doi.org/10.1111/mmi.14067Kai Cai, John Markley. NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis. Molecules 2018, 23 (9) , 2213. https://doi.org/10.3390/molecules23092213Nicholas D. J. Yates, Martin A. Fascione, Alison Parkin. Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces. Chemistry - A European Journal 2018, 24 (47) , 12164-12182. https://doi.org/10.1002/chem.201800750Scot Wherland, Israel Pecht. Radiation chemists look at damage in redox proteins induced by X-rays. Proteins: Structure, Function, and Bioinformatics 2018, 86 (8) , 817-826. https://doi.org/10.1002/prot.25521Firoz Shah Tuglak Khan, Anjani Kumar Pandey, Sankar Prasad Rath. Modulation of iron spin in ethane-bridged diiron(III) porphyrin dimer: anion dependent spin state switching. Journal of Chemical Sciences 2018, 130 (7) https://doi.org/10.1007/s12039-018-1488-2Jianshu Dong, Daisuke Sasaki, Robert R. Eady, Svetlana V. Antonyuk, S. Samar Hasnain. Identification of a tyrosine switch in copper-haem nitrite reductases. IUCrJ 2018, 5 (4) , 510-518. https://doi.org/10.1107/S2052252518008242Ambika Bhagi-Damodaran, Julian H. Reed, Qianhong Zhu, Yelu Shi, Parisa Hosseinzadeh, Braddock A. Sandoval, Kevin A. Harnden, Shuyan Wang, Madeline R. Sponholtz, Evan N. Mirts, Sudharsan Dwaraknath, Yong Zhang, Pierre Moënne-Loccoz, Yi Lu. Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase. Proceedings of the National Academy of Sciences 2018, 115 (24) , 6195-6200. https://doi.org/10.1073/pnas.1720298115Christof M. Jäger, Anna K. Croft. Anaerobic Radical Enzymes for Biotechnology. ChemBioEng Reviews 2018, 5 (3) , 143-162. https://doi.org/10.1002/cben.201800003Smilja Todorovic, Miguel Teixeira. Resonance Raman spectroscopy of Fe–S proteins and their redox properties. JBIC Journal of Biological Inorganic Chemistry 2018, 23 (4) , 647-661. https://doi.org/10.1007/s00775-018-1533-0Julia Stanek, Alexander Hoffmann, Sonja Herres-Pawlis. Renaissance of the entatic state principle. Coordination Chemistry Reviews 2018, 365 , 103-121. https://doi.org/10.1016/j.ccr.2018.03.009Maria Angelica Rea, Christopher D Standish, Jeremiah Shuster, Andrew Bissett, Frank Reith. Progressive biogeochemical transformation of placer gold particles drives compositional changes in associated biofilm communities. FEMS Microbiology Ecology 2018, 94 (6) https://doi.org/10.1093/femsec/fiy080Dapeng Liu, Xiaosong Wang. Hierarchical Self-Assembly Induced by Dilution-Enhanced Hydrophobic Hydration. Chemistry - A European Journal 2018, 24 (26) , 6737-6741. https://doi.org/10.1002/chem.201801213Yunfei Gao, Xiaoqing Hu, Jianli Wang, Huazhong Li, Xiaoyuan Wang. Impact of mycolic acid deficiency on cells of Corynebacterium glutamicum ATCC13869. Biotechnology and Applied Biochemistry 2018, 65 (3) , 435-445. https://doi.org/10.1002/bab.1622Junichi Tanabe, Koji Nakano, Ryutaro Hirata, Toshiki Himeno, Ryoichi Ishimatsu, Toshihiko Imato, Hirotaka Okabe, Naoki Matsuda. Totally synthetic microperoxidase-11. Royal Society Open Science 2018, 5 (5) , 172311. https://doi.org/10.1098/rsos.172311Hyung J Kim. Haem Structure and Function. 2018,,, 1-9. https://doi.org/10.1002/9780470015902.a0000605.pub2Büsra Dereli, Manuel A. Ortuño, Christopher J. Cramer. Accurate Ionization Energies for Mononuclear Copper Complexes Remain a Challenge for Density Functional Theory. ChemPhysChem 2018, 19 (8) , 959-966. https://doi.org/10.1002/cphc.201701334Şükriye Nihan Karuk Elmas, Remziye Güzel, Mehmet Girayhan Say, Arzu Ersoz, Rıdvan Say. Ferritin based bionanocages as novel biomemory device concept. Biosensors and Bioelectronics 2018, 103 , 19-25. https://doi.org/10.1016/j.bios.2017.12.011Xiaojuan Wang, Chuanwan Wei, Ji-Hu Su, Bo He, Ge-Bo Wen, Ying-Wu Lin, Yi Zhang. A Chiral Ligand Assembly That Confers One-Electron O 2 Reduction Activity for a Cu 2+ -Selective Metallohydrogel. Angewandte Chemie 2018, 130 (13) , 3562-3566. https://doi.org/10.1002/ange.201801290Xiaojuan Wang, Chuanwan Wei, Ji-Hu Su, Bo He, Ge-Bo Wen, Ying-Wu Lin, Yi Zhang. A Chiral Ligand Assembly That Confers One-Electron O 2 Reduction Activity for a Cu 2+ -Selective Metallohydrogel. Angewandte Chemie International Edition 2018, 57 (13) , 3504-3508. https://doi.org/10.1002/anie.201801290Pramod Kumar Mehta, Eun-Taex Oh, Heon Joo Park, Keun-Hyeung Lee. Ratiometric detection of Cu+ in aqueous buffered solutions and in live cells using fluorescent peptidyl probe to mimic the binding site of the metalloprotein for Cu+. Sensors and Actuators B: Chemical 2018, 256 , 393-401. https://doi.org/10.1016/j.snb.2017.10.087Richard Grunzke, Volker Hartmann, Thomas Jejkal, Helen Kollai, Christiane Dressler, Julia Dolhoff, Julia Stanek, Hendrik Herold, Alexander Hoffmann, Ralph Muller-Pfefferkorn, Torsten Schrade, Sonja Herres-Pawlis, Gotthard Meinel, Wolfgang E. Nagel. Performance Evaluation of the Metadata-Driven MASi Research Data Management Repository Service. 2018,,, 334-338. https://doi.org/10.1109/PDP2018.2018.00059Elisa Andresen, Edgar Peiter, Hendrik Küpper. Trace metal metabolism in plants. Journal of Experimental Botany 2018, 69 (5) , 909-954. https://doi.org/10.1093/jxb/erx465Caroline L. Monteil, Nicolas Menguy, Sandra Prévéral, Alan Warren, David Pignol, Christopher T. Lefèvre, . Accumulation and Dissolution of Magnetite Crystals in a Magnetically Responsive Ciliate. Applied and Environmental Microbiology 2018, 84 (8) , e02865-17. https://doi.org/10.1128/AEM.02865-17Hagai Raanan, Douglas H. Pike, Eli K. Moore, Paul G. Falkowski, Vikas Nanda. Modular origins of biological electron transfer chains. Proceedings of the National Academy of Sciences 2018, 115 (6) , 1280-1285. https://doi.org/10.1073/pnas.1714225115Huihui Fu, Lulu Liu, Ziyang Dong, Shupan Guo, Haichun Gao, . Dissociation between Iron and Heme Biosyntheses Is Largely Accountable for Respiration Defects of Shewanella oneidensis fur Mutants. Applied and Environmental Microbiology 2018, 84 (8) , e00039-18. https://doi.org/10.1128/AEM.00039-18Jeong Yeon Do, No-Kuk Park, Tae Jin Lee, Sang Tae Lee, Misook Kang. Effective hydrogen productions from propane steam reforming over spinel-structured metal-manganese oxide redox couple catalysts. International Journal of Energy Research 2018, 42 (2) , 429-446. https://doi.org/10.1002/er.3812Pirmin Stüble, Simon Peschke, Dirk Johrendt, Caroline Röhr. Na7[Fe2S6] , Na2[FeS2] and Na2[FeSe2] : New ‘reduced’ sodium chalcogenido ferrates. Journal of Solid State Chemistry 2018, 258 , 416-430. https://doi.org/10.1016/j.jssc.2017.10.033Stella Maria Barrouin-Melo, Yadira Alejandra Morejón Terán, Johanna Anturaniemi, Anna Katrina Hielm-Björkman. Interaction Between Nutrition and Metabolism. 2018,,, 29-114. https://doi.org/10.1007/978-3-319-74932-7_2Peter M. H. Kroneck. Walking the seven lines: binuclear copper A in cytochrome c oxidase and nitrous oxide reductase. JBIC Journal of Biological Inorganic Chemistry 2018, 23 (1) , 27-39. https://doi.org/10.1007/s00775-017-1510-zF. Melin, A. Nikolaev, P. Hellwig. Redox Activity of Cytochromes from the Respiratory Chain. 2018,,, 451-469. https://doi.org/10.1016/B978-0-12-409547-2.13899-5Shuai Liang, Saad Shaaban, Nai-Wei Liu, Kamil Hofman, Georg Manolikakes. Recent Advances in the Synthesis of C–S Bonds via Metal-Catalyzed or -Mediated Functionalization of C–H Bonds. 2018,,, 135-207. https://doi.org/10.1016/bs.adomc.2018.02.001Oleksandra Veselska, Aude Demessence. d10 coinage metal organic chalcogenolates: From oligomers to coordination polymers. Coordination Chemistry Reviews 2018, 355 , 240-270. https://doi.org/10.1016/j.ccr.2017.08.014Adalgisa Sinicropi. DFT modeling of structures and redox potentials of wild-type, Nickel-substituted and mutated (N47S/M121L, HPAz) Azurin. Inorganica Chimica Acta 2018, 470 , 360-364. https://doi.org/10.1016/j.ica.2017.08.041Ksenia A. Myannik, Elena K. Beloglazkina, Anna A. Moiseeva, Tatiana K. Baryshnikova, Vladimir N. Yarovenko, Mikhail M. Krayushkin. Synthesis and electrochemical study of 2-carbamoyl-4,5-dihydro-1,3,4-thiadiazole-containing ligands and their complexes with Cu ii , Co ii and Ni ii. Mendeleev Communications 2018, 28 (1) , 79-80. https://doi.org/10.1016/j.mencom.2018.01.026Remziye Güzel, Arzu Ersöz, Recep Ziyadanoğulları, Rıdvan Say. Nano-hemoglobin film based sextet state biomemory device by cross-linked photosensitive hapten monomer. Talanta 2018, 176 , 85-91. https://doi.org/10.1016/j.talanta.2017.08.014Candan Ariöz, Pernilla Wittung-Stafshede. Folding of copper proteins: role of the metal?. Quarterly Reviews of Biophysics 2018, 51 https://doi.org/10.1017/S0033583518000021Teera Chantarojsiri, Joseph W. Ziller, Jenny Y. Yang. Incorporation of redox-inactive cations promotes iron catalyzed aerobic C–H oxidation at mild potentials. Chemical Science 2018, 9 (9) , 2567-2574. https://doi.org/10.1039/C7SC04486KRudra N. Samajdar, Dhivya Manogaran, S. Yashonath, Aninda J. Bhattacharyya. Using porphyrin–amino acid pairs to model the electrochemistry of heme proteins: experimental and theoretical investigations. Physical Chemistry Chemical Physics 2018, 20 (15) , 10018-10029. https://doi.org/10.1039/C8CP00605ANikolai Lebedev, Igor Griva, Anders Blom, Leonard M. Tender. Effect of iron doping on protein molecular conductance. Physical Chemistry Chemical Physics 2018, 20 (20) , 14072-14081. https://doi.org/10.1039/C8CP00656CHai-Xiao Liu, Lianzhi Li, Bo He, Shu-Qin Gao, Ge-Bo Wen, Ying-Wu Lin. Neuroglobin is capable of self-oxidation of methionine64 introduced at the heme axial position. Dalton Transactions 2018, 47 (32) , 10847-10852. https://doi.org/10.1039/C8DT02397BAndrés Espinoza-Cara, Ulises Zitare, Damián Alvarez-Paggi, Sebastián Klinke, Lisandro H. Otero, Daniel H. Murgida, Alejandro J. Vila. Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis. Chemical Science 2018, 9 (32) , 6692-6702. https://doi.org/10.1039/C8SC01444BDaniel R. Martin, Dmitry V. Matyushov. Electron-transfer chain in respiratory complex I. Scientific Reports 2017, 7 (1) https://doi.org/10.1038/s41598-017-05779-yK. A. Motovilov, M. Savinov, E. S. Zhukova, A. A. Pronin, Z. V. Gagkaeva, V. Grinenko, K. V. Sidoruk, T. A. Voeikova, P. Yu. Barzilovich, A. K. Grebenko, S. V. Lisovskii, V. I. Torgashev, P. Bednyakov, J. Pokorný, M. Dressel, B. P. Gorshunov. Observation of dielectric universalities in albumin, cytochrome C and Shewanella oneidensis MR-1 extracellular matrix. Scientific Reports 2017, 7 (1) https://doi.org/10.1038/s41598-017-15693-yFelix Koch, Andreas Berkefeld, Bernd Speiser, Hartmut Schubert. Mechanistic Aspects of Redox-Induced Assembly and Disassembly of S-Bridged [2M-2S] Structures. Chemistry - A European Journal 2017, 23 (65) , 16681-16690. https://doi.org/10.1002/chem.201704599Julia Stanek, Nina Sackers, Fabian Fink, Melanie Paul, Laurens Peters, Richard Grunzke, Alexander Hoffmann, Sonja Herres-Pawlis. Copper Guanidinoquinoline Complexes as Entatic State Models of Electron-Transfer Proteins. Chemistry - A European Journal 2017, 23 (62) , 15738-15745. https://doi.org/10.1002/chem.201703261Mateus Ribeiro da Silva, Carla Andreia Freixo Portela, Silvia Maria Ferreira Albani, Paola Rizzo de Paiva, Martha Massako Tanizaki, Teresa Cristina Zangirolami. Experimental design and metabolic flux analysis tools to optimize industrially relevant Haemophilus influenzae type b growth medium. Biotechnology Progress 2017, 33 (6) , 1508-1519. https://doi.org/10.1002/btpr.2546Sergi Garcia-Manyes, Amy E. M. Beedle. Steering chemical reactions with force. Nature Reviews Chemistry 2017, 1 (11) https://doi.org/10.1038/s41570-017-0083Younis Ahmad Pandit, Sarnali Sanfui, Sankar Prasad Rath. Intermacrocyclic Interaction Triggers Facile One-Pot Synthesis of a Chlorin-Porphyrin Heterodimer. Chemistry - A European Journal 2017, 23 (54) , 13415-13422. https://doi.org/10.1002/chem.201701943Duobin Chao, Mengying Zhao. Robust Cooperative Photo-oxidation of Sulfides without Sacrificial Reagent under Air Using a Dinuclear Ru II -Cu II Assembly. ChemSusChem 2017, 10 (17) , 3358-3362. https://doi.org/10.1002/cssc.201700930Vera Engelbrecht, Patricia Rodríguez-Maciá, Julian Esselborn, Anne Sawyer, Anja Hemschemeier, Olaf Rüdiger, Wolfgang Lubitz, Martin Winkler, Thomas Happe. The structurally unique photosynthetic Chlorella variabilis NC64A hydrogenase does not interact with plant-type ferredoxins. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2017, 1858 (9) , 771-778. https://doi.org/10.1016/j.bbabio.2017.06.004Eli K. Moore, Benjamin I. Jelen, Donato Giovannelli, Hagai Raanan, Paul G. Falkowski. Metal availability and the expanding network of microbial metabolisms in the Archaean eon. Nature Geoscience 2017, 10 (9) , 629-636. https://doi.org/10.1038/ngeo3006Akhil Kumar Singh, Firoz Shah Tuglak Khan, Sankar Prasad Rath. Silver(III)⋅⋅⋅Silver(III) Interactions that Stabilize the syn Form in a Porphyrin Dimer Upon Oxidation. Angewandte Chemie 2017, 129 (30) , 8975-8980. https://doi.org/10.1002/ange.201705108Akhil Kumar Singh, Firoz Shah Tuglak Khan, Sankar Prasad Rath. Silver(III)⋅⋅⋅Silver(III) Interactions that Stabilize the syn Form in a Porphyrin Dimer Upon Oxidation. Angewandte Chemie International Edition 2017, 56 (30) , 8849-8854. https://doi.org/10.1002/anie.201705108Michael W. Mara, Ryan G. Hadt, Marco Eli Reinhard, Thomas Kroll, Hyeongtaek Lim, Robert W. Hartsock, Roberto Alonso-Mori, Matthieu Chollet, James M. Glownia, Silke Nelson, Dimosthenis Sokaras, Kristjan Kunnus, Keith O. Hodgson, Britt Hedman, Uwe Bergmann, Kelly J. Gaffney, Edward I. Solomon. Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy. Science 2017, 356 (6344) , 1276-1280. https://doi.org/10.1126/science.aam6203Manu Sánchez, Laura Sabio, Natividad Gálvez, Mercè Capdevila, Jose M. Dominguez‐Vera. Iron chemistry at the service of life. IUBMB Life 2017, 69 (6) , 382-388. https://doi.org/10.1002/iub.1602Licia Paltrinieri, Giulia Di Rocco, Gianantonio Battistuzzi, Marco Borsari, Marco Sola, Antonio Ranieri, Laura Zanetti-Polzi, Isabella Daidone, Carlo Augusto Bortolotti. Computational evidence support the hypothesis of neuroglobin also acting as an electron transfer species. JBIC Journal of Biological Inorganic Chemistry 2017, 22 (4) , 615-623. https://doi.org/10.1007/s00775-017-1455-2Pinapeddavari Mayuri, Natarajan Saravanan, Annamalai Senthil Kumar. A bioinspired copper 2,2-bipyridyl complex immobilized MWCNT modified electrode prepared by a new strategy for elegant electrocatalytic reduction and sensing of hydrogen peroxide. Electrochimica Acta 2017, 240 , 522-533. https://doi.org/10.1016/j.electacta.2017.04.082, , Lewis A. Churchfield, Athira George, F. Akif Tezcan. Repurposing proteins for new bioinorganic functions. Essays in Biochemistry 2017, 61 (2) , 245-258. https://doi.org/10.1042/EBC20160068Magali Roger, Giuliano Sciara, Frédéric Biaso, Elisabeth Lojou, Xie Wang, Marielle Bauzan, Marie-Thérèse Giudici-Orticoni, Alejandro J. Vila, Marianne Ilbert. Impact of copper ligand mutations on a cupredoxin with a green copper center. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2017, 1858 (5) , 351-359. https://doi.org/10.1016/j.bbabio.2017.02.007Shun Ohta, Yasuhiro Ohki. Impact of ligands and media on the structure and properties of biological and biomimetic iron-sulfur clusters. Coordination Chemistry Reviews 2017, 338 , 207-225. https://doi.org/10.1016/j.ccr.2017.02.018Guofu Li, Haiyan Xue, Zeng Fan, Yun Bai. Impact of heme on specific antibody production in mice: promotive, inhibitive or null outcome is determined by its concentration. Heliyon 2017, 3 (5) , e00303. https://doi.org/10.1016/j.heliyon.2017.e00303Gunseli Bayram Akcapinar, Osman Ugur Sezerman. Computational approaches for de novo design and redesign of metal-binding sites on proteins. Bioscience Reports 2017, 37 (2) https://doi.org/10.1042/BSR20160179Christina Ferousi, Simon Lindhoud, Frauke Baymann, Boran Kartal, Mike SM Jetten, Joachim Reimann. Iron assimilation and utilization in anaerobic ammonium oxidizing bacteria. Current Opinion in Chemical Biology 2017, 37 , 129-136. https://doi.org/10.1016/j.cbpa.2017.03.009Ying-Wu Lin. Rational design of metalloenzymes: From single to multiple active sites. Coordination Chemistry Reviews 2017, 336 , 1-27. https://doi.org/10.1016/j.ccr.2017.01.001Tapas Guchhait, Sujit Sasmal, Firoz Shah Tuglak Khan, Sankar Prasad Rath. Oxo- and hydroxo-bridged diiron(III) porphyrin dimers: Inorganic and bio-inorganic perspectives and effects of intermacrocyclic interactions. Coordination Chemistry Reviews 2017, 337 , 112-144. https://doi.org/10.1016/j.ccr.2017.02.008Piero Zanello. The competition between chemistry and biology in assembling iron–sulfur derivatives. Molecular structures and electrochemistry. Part V. {[Fe4S4](SCysγ)4} proteins. Coordination Chemistry Reviews 2017, 335 , 172-227. https://doi.org/10.1016/j.ccr.2016.10.003Shan Hu, Bo He, Xiao-Juan Wang, Shu-Qin Gao, Ge-Bo Wen, Ying-Wu Lin. Stabilization of cytochrome b 5 by a conserved tyrosine in the secondary sphere of heme active site: A spectroscopic and computational study. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2017, 174 , 118-123. https://doi.org/10.1016/j.saa.2016.11.032Ilya V. Kublanov, Olga M. Sigalova, Sergey N. Gavrilov, Alexander V. Lebedinsky, Christian Rinke, Olga Kovaleva, Nikolai A. Chernyh, Natalia Ivanova, Chris Daum, T.B.K. Reddy, Hans-Peter Klenk, Stefan Spring, Markus Göker, Oleg N. Reva, Margarita L. Miroshnichenko, Nikos C. Kyrpides, Tanja Woyke, Mikhail S. Gelfand, Elizaveta A. Bonch-Osmolovskaya. Genomic Analysis of Caldithrix abyssi, the Thermophilic Anaerobic Bacterium of the Novel Bacterial Phylum Calditrichaeota. Frontiers in Microbiology 2017, 8 https://doi.org/10.3389/fmicb.2017.00195Marcin Sarewicz, Łukasz Bujnowicz, Satarupa Bhaduri, Sandeep K. Singh, William A. Cramer, Artur Osyczka. Metastable radical state, nonreactive with oxygen, is inherent to catalysis by respiratory and photosynthetic cytochromes bc1 / b6f. Proceedings of the National Academy of Sciences 2017, 114 (6) , 1323-1328. https://doi.org/10.1073/pnas.1618840114Yang Yu, Igor D. Petrik, Kelly N. Chacón, Parisa Hosseinzadeh, Honghui Chen, Ninian J. Blackburn, Yi Lu. Effect of circular permutation on the structure and function of type 1 blue copper center in azurin. Protein Science 2017, 26 (2) , 218-226. https://doi.org/10.1002/pro.3071Alexander Oppermann, Christoph Wehrhahn, Ulrich Flörke, Sonja Herres-Pawlis, Gerald Henkel. Direct Electrochemical Synthesis of an Unusual Complex Salt: Almost Structural Identity - Different Charge. Zeitschrift für anorganische und allgemeine Chemie 2017, 643 (3) , 266-275. https://doi.org/10.1002/zaac.201600408Yang Yu, Chang Cui, Jiangyun Wang, Yi Lu. Biosynthetic approach to modeling and understanding metalloproteins using unnatural amino acids. Science China Chemistry 2017, 60 (2) , 188-200. https://doi.org/10.1007/s11426-016-0343-2R. Martin Roop II, Clayton C. Caswell. Introduction and Overview. 2017,,, 1-8. https://doi.org/10.1007/978-3-319-53622-4_1Abdelwahab Rai, Elhafid Nabti. Plant Growth-Promoting Bacteria: Importance in Vegetable Production. 2017,,, 23-48. https://doi.org/10.1007/978-3-319-54401-4_2Felix Bulcke, Ralf Dringen, Ivo Florin Scheiber. Neurotoxicity of Copper. 2017,,, 313-343. https://doi.org/10.1007/978-3-319-60189-2_16Zahra B. Dizicheh, Nicholas Halloran, William Asma, Giovanna Ghirlanda. De Novo Design of Iron–Sulfur Proteins. 2017,,, 33-53. https://doi.org/10.1016/bs.mie.2017.07.014Ram Chandra Maji, Partha Pratim Das, Anirban Bhandari, Saikat Mishra, Milan Maji, Kamran B. Ghiassi, Marilyn M. Olmstead, Apurba K. Patra. Mixed valence copper–sulfur clusters of highest nuclearity: a Cu 8 wheel and a Cu 16 nanoball. Chemical Communications 2017, 53 (23) , 3334-3337. https://doi.org/10.1039/C6CC08301CCheng Hu, Yang Yu, Jiangyun Wang. Improving artificial metalloenzymes' activity by optimizing electron transfer. Chemical Communications 2017, 53 (30) , 4173-4186. https://doi.org/10.1039/C6CC09921AFiroz Shah Tuglak Khan, Tapas Guchhait, Sujit Sasmal, Sankar Prasad Rath. Hydroxo-bridged diiron( iii ) and dimanganese( iii ) bisporphyrins: modulation of metal spins by counter anions. Dalton Transactions 2017, 46 (4) , 1012-1037. https://doi.org/10.1039/C6DT03829HBin Yao, Praveen Kolla, Ranjit Koodali, Yichun Ding, Selvaratnam Balaranjan, Sunav Shrestha, Alevtina Smirnova. Enzymatic decomposition and electrochemical study of alkali lignin by laccase (Trametes versicolor) in the presence of a natural mediator (methyl syringate). New Journal of Chemistry 2017, 41 (3) , 958-964. https://doi.org/10.1039/C6NJ03104HHonghui Chen, Binbin Su, Tongtong Zhang, Aiping Huang, Haiping Liu, Yang Yu, Jiangyun Wang. Engineering the metal-binding loop at a type 1 copper center by circular permutation. RSC Advances 2017, 7 (88) , 56093-56098. https://doi.org/10.1039/C7RA11512AJing Yang, Xueli Zhang, Yiying Zhu, Emily Lenczowski, Yanli Tian, Jian Yang, Can Zhang, Markus Hardt, Chunhua Qiao, Rudolph E. Tanzi, Anna Moore, Hui Ye, Chongzhao Ran. The double-edged role of copper in the fate of amyloid beta in the presence of anti-oxidants. Chemical Science 2017, 8 (9) , 6155-6164. https://doi.org/10.1039/C7SC01787ALeonie Kertess, Agnieszka Adamska-Venkatesh, Patricia Rodríguez-Maciá, Olaf Rüdiger, Wolfgang Lubitz, Thomas Happe. Influence of the [4Fe–4S] cluster coordinating cysteines on active site maturation and catalytic properties of C. reinhardtii [FeFe]-hydrogenase. Chemical Science 2017, 8 (12) , 8127-8137. https://doi.org/10.1039/C7SC03444JLei-Bin Wu, Ke-Jie Du, Chang-Ming Nie, Shu-Qin Gao, Ge-Bo Wen, Xiangshi Tan, Ying-Wu Lin. Peroxidase activity enhancement of myoglobin by two cooperative distal histidines and a channel to the heme pocket. Journal of Molecular Catalysis B: Enzymatic 2016, 134 , 367-371. https://doi.org/10.1016/j.molcatb.2016.08.018Yuchen Liu, David J. Vinyard, Megan E. Reesbeck, Tateki Suzuki, Kasidet Manakongtreecheep, Patrick L. Holland, Gary W. Brudvig, Dieter Söll. A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes. Proceedings of the National Academy of Sciences 2016, 113 (45) , 12703-12708. https://doi.org/10.1073/pnas.1615732113Alexander Hoffmann, Julia Stanek, Benjamin Dicke, Laurens Peters, Benjamin Grimm-Lebsanft, Alina Wetzel, Anton Jesser, Matthias Bauer, Manuel Gnida, Wolfram Meyer-Klaucke, Michael Rübhausen, Sonja Herres-Pawlis. Implications of Guanidine Substitution on Copper Complexes as Entatic-State Models. European Journal of Inorganic Chemistry 2016, 2016 (29) , 4731-4743. https://doi.org/10.1002/ejic.201600655Edward I. Solomon, Ryan G. Hadt, Benjamin E. R. Snyder. Activating Metal Sites for Biological Electron Transfer. Israel Journal of Chemistry 2016, 56 (9-10) , 649-659. https://doi.org/10.1002/ijch.201600016Kara L. Bren. Going with the Electron Flow: Heme Electronic Structure and Electron Transfer in Cytochrome c. Israel Journal of Chemistry 2016, 56 (9-10) , 693-704. https://doi.org/10.1002/ijch.201600021Elizabeth O'Brien, Rebekah M. B. Silva, Jacqueline K. Barton. Redox Signaling through DNA. Israel Journal of Chemistry 2016, 56 (9-10) , 705-723. https://doi.org/10.1002/ijch.201600022Atif Mahammed, Zeev Gross. Metallocorroles as Electrocatalysts for the Oxygen Reduction Reaction (ORR). Israel Journal of Chemistry 2016, 56 (9-10) , 756-762. https://doi.org/10.1002/ijch.201600027Chiara Baldacchini, Anna Rita Bizzarri, Salvatore Cannistraro. Electron transfer, conduction and biorecognition properties of the redox metalloprotein Azurin assembled onto inorganic substrates. European Polymer Journal 2016, 83 , 407-427. https://doi.org/10.1016/j.eurpolymj.2016.04.030Benjamin I. Jelen, Donato Giovannelli, Paul G. Falkowski. The Role of Microbial Electron Transfer in the Coevolution of the Biosphere and Geosphere. Annual Review of Microbiology 2016, 70 (1) , 45-62. https://doi.org/10.1146/annurev-micro-102215-095521Mohammadhasan Dinpajooh, Daniel R. Martin, Dmitry V. Matyushov. Polarizability of the active site of cytochrome c reduces the activation barrier for electron transfer. Scientific Reports 2016, 6 (1) https://doi.org/10.1038/srep28152Alexander Oppermann, Regina Dick, Christoph Wehrhahn, Ulrich Flörke, Sonja Herres-Pawlis, Gerald Henkel. Copper(I) Thiolate Heteroadamantane Cage Structures with Relevance to Metalloproteins. European Journal of Inorganic Chemistry 2016, 2016 (23) , 3744-3755. https://doi.org/10.1002/ejic.201600247Wagner S. Terra, Sarah S. Ferreira, Rafael O. Costa, Luisa L. Mendes, Roberto W.A. Franco, Adailton J. Bortoluzzi, Jackson A.L.C. Resende, Christiane Fernandes, Adolfo Horn. Evaluating the influence of the diamine unit (ethylenediamine, piperazine and homopiperazine) on the molecular structure, physical chemical properties and superoxide dismutase activity of copper complexes. Inorganica Chimica Acta 2016, 450 , 353-363. https://doi.org/10.1016/j.ica.2016.06.024Lei-Bin Wu, Hong Yuan, Shu-Qin Gao, Yong You, Chang-Ming Nie, Ge-Bo Wen, Ying-Wu Lin, Xiangshi Tan. Regulating the nitrite reductase activity of myoglobin by redesigning the heme active center. Nitric Oxide 2016, 57 , 21-29. https://doi.org/10.1016/j.niox.2016.04.007Shiyu Zhang, Marie M. Melzer, S. Nermin Sen, Nihan Çelebi-Ölçüm, Timothy H. Warren. A motif for reversible nitric oxide interactions in metalloenzymes. Nature Chemistry 2016, 8 (7) , 663-669. https://doi.org/10.1038/nchem.2502Xiao-Gang Shu, Ji-Hu Su, Ke-Jie Du, Yong You, Shu-Qin Gao, Ge-Bo Wen, Xiangshi Tan, Ying-Wu Lin. Rational Design of Dual Active Sites in a Single Protein Scaffold: A Case Study of Heme Protein in Myoglobin. ChemistryOpen 2016, 5 (3) , 192-196. https://doi.org/10.1002/open.201500224. Metal Sulfides in the Environment and in Bioinorganic Chemistry. 2016,,, 390-405. https://doi.org/10.1002/9781118851432.ch12Parisa Hosseinzadeh, Yi Lu. Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2016, 1857 (5) , 557-581. https://doi.org/10.1016/j.bbabio.2015.08.006Antonio Rosato, Yana Valasatava, Claudia Andreini. Minimal Functional Sites in Metalloproteins and Their Usage in Structural Bioinformatics. International Journal of Molecular Sciences 2016, 17 (5) , 671. https://doi.org/10.3390/ijms17050671Chunqiang Zhang, Fan Zhang, Ping Zhou, Caiguo Zhang. Functional role of metalloproteins in genome stability. Frontiers in Biology 2016, 11 (2) , 119-131. https://doi.org/10.1007/s11515-016-1392-4Zhu-Jun Liu, Xin-Long Wang, Chao Qin, Zhi-Ming Zhang, Yang-Guang Li, Wei-Lin Chen, En-Bo Wang. Polyoxometalate-assisted synthesis of transition-metal cubane clusters as artificial mimics of the oxygen-evolving center of photosystem II. Coordination Chemistry Reviews 2016, 313 , 94-110. https://doi.org/10.1016/j.ccr.2015.12.006David C Gillan. Metal resistance systems in cultivated bacteria: are they found in complex communities?. Current Opinion in Biotechnology 2016, 38 , 123-130. https://doi.org/10.1016/j.copbio.2016.01.012Yuan Zhao, Ke-Jie Du, Shu-Qin Gao, Bo He, Ge-Bo Wen, Xiangshi Tan, Ying-Wu Lin. Distinct mechanisms for DNA cleavage by myoglobin with a designed heme active center. Journal of Inorganic Biochemistry 2016, 156 , 113-121. https://doi.org/10.1016/j.jinorgbio.2016.01.004Felix Bulcke, Ralf Dringen. Handling of Copper and Copper Oxide Nanoparticles by Astrocytes. Neurochemical Research 2016, 41 (1-2) , 33-43. https://doi.org/10.1007/s11064-015-1688-9Parisa Hosseinzadeh, Nicholas M. Marshall, Kelly N. Chacón, Yang Yu, Mark J. Nilges, Siu Yee New, Stoyan A. Tashkov, Ninian J. Blackburn, Yi Lu. Design of a single protein that spans the entire 2-V range of physiological redox potentials. Proceedings of the National Academy of Sciences 2016, 113 (2) , 262-267. https://doi.org/10.1073/pnas.1515897112Dayn Joseph Sommer, Rafael Alcala-Torano, Zahra Bahrami Dizicheh, Giovanna Ghirlanda. Design of Redox-Active Peptides: Towards Functional Materials. 2016,,, 215-243. https://doi.org/10.1007/978-3-319-39196-0_10Gábor Bernát, Dirk Schneider, Matthias Rögner. Alternative Rieske Iron-Sulfur Subunits and Small Polypeptides of Cyanobacterial Cytochrome b 6 f Complexes. 2016,,, 265-279. https://doi.org/10.1007/978-94-017-7481-9_13U. Ryde. QM/MM Calculations on Proteins. 2016,,, 119-158. https://doi.org/10.1016/bs.mie.2016.05.014A. Bhagi-Damodaran, P. Hosseinzadeh, E. Mirts, J. Reed, I.D. Petrik, Y. Lu. Design of Heteronuclear Metalloenzymes. 2016,,, 501-537. https://doi.org/10.1016/bs.mie.2016.05.050R. Alcala-Torano, D.J. Sommer, Z. Bahrami Dizicheh, G. Ghirlanda. Design Strategies for Redox Active Metalloenzymes. 2016,,, 389-416. https://doi.org/10.1016/bs.mie.2016.06.001Mónica N. Alves, Ana P. Fernandes, Carlos A. Salgueiro, Catarina M. Paquete. Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2016, 1857 (1) , 7-13. https://doi.org/10.1016/j.bbabio.2015.09.010Liuming Yan, Yi Lu, Xuejiao Li. A density functional theory protocol for the calculation of redox potentials of copper complexes. Physical Chemistry Chemical Physics 2016, 18 (7) , 5529-5536. https://doi.org/10.1039/C5CP06638GHiroshi Fujii, Daisuke Yamaki, Takashi Ogura, Masahiko Hada. The functional role of the structure of the dioxo-isobacteriochlorin in the catalytic site of cytochrome cd 1 for the reduction of nitrite. Chemical Science 2016, 7 (4) , 2896-2906. https://doi.org/10.1039/C5SC04825GMatthew D. Yates, Brian J. Eddie, Nicholas J. Kotloski, Nikolai Lebedev, Anthony P. Malanoski, Baochuan Lin, Sarah M. Strycharz-Glaven, Leonard M. Tender. Toward understanding long-distance extracellular electron transport in an electroautotrophic microbial community. Energy & Environmental Science 2016, 9 (11) , 3544-3558. https://doi.org/10.1039/C6EE02106ASaumen Chakraborty, Reginaldo C. Rocha, Anil Desireddy, Kateryna Artyushkova, Timothy C. Sanchez, Albert T. Perry, Plamen Atanassov, Jennifer S. Martinez. Gold nanocluster formation using morpholino oligomer as template and assembly agent within hybrid bio-nanomaterials. RSC Advances 2016, 6 (93) , 90624-90630. https://doi.org/10.1039/C6RA16891DQingtao Meng, Hongmin Jia, Peter Succar, Liang Zhao, Run Zhang, Chunying Duan, Zhiqiang Zhang. A highly selective and sensitive ON–OFF–ON fluorescence chemosensor for cysteine detection in endoplasmic reticulum. Biosensors and Bioelectronics 2015, 74 , 461-468. https://doi.org/10.1016/j.bios.2015.06.077Catarina Paquete, Bruno Fonseca, Ricardo Louro. Multi-Electron Transfer in Biological Systems. 2015,,, 1-34. https://doi.org/10.1201/b19087-2Kira S. Makarova, Michael Y. Galperin, Eugene V. Koonin. Comparative genomic analysis of evolutionarily conserved but functionally uncharacterized membrane proteins in archaea: Prediction of novel components of secretion, membrane remodeling and glycosylation systems. Biochimie 2015, 118 , 302-312. https://doi.org/10.1016/j.biochi.2015.01.004Amy E. M. Beedle, Ainhoa Lezamiz, Guillaume Stirnemann, Sergi Garcia-Manyes. The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins. Nature Communications 2015, 6 (1) https://doi.org/10.1038/ncomms8894Matthias Knop, Pascal Engi, Roxana Lemnaru, Florian P. Seebeck. In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I). ChemBioChem 2015, 16 (15) , 2147-2150. https://doi.org/10.1002/cbic.201500322María F. Molinas, Leandro Benavides, María A. Castro, Daniel H. Murgida. Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily. Bioelectrochemistry 2015, 105 , 25-33. https://doi.org/10.1016/j.bioelechem.2015.05.005Dayn Joseph Sommer, Anindya Roy, Andrei Astashkin, Giovanna Ghirlanda. Modulation of cluster incorporation specificity in a de novo iron-sulfur cluster binding peptide. Biopolymers 2015, 104 (4) , 412-418. https://doi.org/10.1002/bip.22635Megan E. Reesbeck, Meghan M. Rodriguez, William W. Brennessel, Brandon Q. Mercado, David Vinyard, Patrick L. Holland. Oxidized and reduced [2Fe–2S] clusters from an iron(I) synthon. JBIC Journal of Biological Inorganic Chemistry 2015, 20 (5) , 875-883. https://doi.org/10.1007/s00775-015-1272-4Wen Li, Wei Bing, Sa Huang, Jinsong Ren, Xiaogang Qu. Mussel Byssus-Like Reversible Metal-Chelated Supramolecular Complex Used for Dynamic Cellular Surface Engineering and Imaging. Advanced Functional Materials 2015, 25 (24) , 3775-3784. https://doi.org/10.1002/adfm.201500039Debangsu Sil, Sankar Prasad Rath. An ethane-bridged porphyrin dimer as a model of di-heme proteins: inorganic and bioinorganic perspectives and consequences of heme–heme interactions. Dalton Transactions 2015, 44 (37) , 16195-16211. https://doi.org/10.1039/C5DT00947BYi Yu, Taniyuki Furuyama, Juan Tang, Zhuo-Yan Wu, Jia-Zhen Chen, Nagao Kobayashi, Jun-Long Zhang. Stable iso-bacteriochlorin mimics from porpholactone: effect of a β-oxazolone moiety on the frontier π-molecular orbitals. Inorganic Chemistry Frontiers 2015, 2 (7) , 671-677. https://doi.org/10.1039/C5QI00054HPrashant D. Wadhavane, Lingaraju Gorla, Armando Ferrer, Belén Altava, M. Isabel Burguete, M. Ángeles Izquierdo, Santiago V. Luis. Coordination behaviour of new open chain and macrocyclic peptidomimetic compounds with copper( ii ). RSC Advances 2015, 5 (89) , 72579-72589. https://doi.org/10.1039/C5RA15852DHeather R. Williamson, Brian A. Dow, Victor L. Davidson. Mechanisms for control of biological electron transfer reactions. Bioorganic Chemistry 2014, 57 , 213-221. https://doi.org/10.1016/j.bioorg.2014.06.006Selena L. Rice, Matthew R. Preimesberger, Eric A. Johnson, Juliette T.J. Lecomte. Introduction of a covalent histidine–heme linkage in a hemoglobin: A promising tool for heme protein engineering. Journal of Inorganic Biochemistry 2014, 141 , 198-207. https://doi.org/10.1016/j.jinorgbio.2014.09.009Yoshikazu Ninomiya, Masatoshi Kozaki, Shuichi Suzuki, Keiji Okada. Allosteric Regulation of the Ligand-Binding Ability of Zinc Porphyrins with Sterically Bulky Shielding Units by Metal Complexation. Bulletin of the Chemical Society of Japan 2014, 87 (11) , 1195-1201. https://doi.org/10.1246/bcsj.20140197Ying-Wu Lin, Xiao-Gang Shu, Ke-Jie Du, Chang-Ming Nie, Ge-Bo Wen. Computational insight into nitration of human myoglobin. Computational Biology and Chemistry 2014, 52 , 60-65. https://doi.org/10.1016/j.compbiolchem.2014.09.004Saumen Chakraborty, Parisa Hosseinzadeh, Yi Lu. Metalloprotein Design and Engineering. 2014,,, 1-51. https://doi.org/10.1002/9781119951438.eibc0259.pub2Namik Akkilic, Fenna van der Grient, Muhammad Kamran, Nusrat J. M. Sanghamitra. Chemically-induced redox switching of a metalloprotein reveals thermodynamic and kinetic heterogeneity, one molecule at a time. Chem. Commun. 2014, 50 (93) , 14523-14526. https://doi.org/10.1039/C4CC06334A

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