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A."},{"issue":"6352","key":"10.1016\/B978-0-12-823144-9.00116-3_bib0915","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1126\/science.aan0425","article-title":"Methanogenic Heterodisulfide Reductase (HdrABC-MvhAGD) Uses Two Noncubane [4Fe-4S] Clusters for Reduction","volume":"357","author":"Wagner","year":"2017","journal-title":"Science"},{"issue":"12","key":"10.1016\/B978-0-12-823144-9.00116-3_bib0920","doi-asserted-by":"crossref","first-page":"4083","DOI":"10.1039\/f19898504083","article-title":"Novel Electron Paramagnetic Resonance Signals from an Fe\/S Protein Containing Six Iron Atoms","volume":"85","author":"Hagen","year":"1989","journal-title":"J.\u00a0Chem. Soc., Faraday Trans. 1"},{"issue":"7","key":"10.1016\/B978-0-12-823144-9.00116-3_bib0925","doi-asserted-by":"crossref","first-page":"4489","DOI":"10.1016\/S0021-9258(18)42859-1","article-title":"Direct Spectroscopic Evidence for the Presence of a 6Fe Cluster in an Iron-Sulfur Protein Isolated from Desulfovibrio desulfuricans (ATCC 27774)","volume":"267","author":"Moura","year":"1992","journal-title":"J.\u00a0Biol. Chem."},{"issue":"1","key":"10.1016\/B978-0-12-823144-9.00116-3_bib0930","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1007\/s007750050210","article-title":"The \u201cPrismane\u201d Protein Resolved: X-Ray Structure at 1.7\u00c5 and Multiple Spectroscopy of Two Novel 4Fe Clusters","volume":"3","author":"Arendsen","year":"1998","journal-title":"J.\u00a0Biol. Inorg. 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Microbiol."},{"issue":"21","key":"10.1016\/B978-0-12-823144-9.00116-3_bib0995","doi-asserted-by":"crossref","first-page":"3075","DOI":"10.1002\/1873-3468.13539","article-title":"EPR Spectroscopy of Putative Enzyme Intermediates in the NO Reductase and the Auto-Nitrosylation Reaction of Desulfovibrio Vulgaris Hybrid Cluster Protein","volume":"593","author":"Hagen","year":"2019","journal-title":"FEBS Lett."},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1000","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/S0959-440X(96)80003-0","article-title":"The Relationship between Structure and Function for the Sulfite Reductases","volume":"6","author":"Crane","year":"1996","journal-title":"Curr. Opin. Struct. Biol."},{"issue":"5233","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1005","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1126\/science.270.5233.59","article-title":"Sulfite Reductase Structure at 1.6\u00a0\u00c5: Evolution and Catalysis for Reduction of Inorganic Anions","volume":"270","author":"Crane","year":"1995","journal-title":"Science"},{"issue":"15","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1010","doi-asserted-by":"crossref","first-page":"3538","DOI":"10.1021\/bi00258a003","article-title":"Electron Paramagnetic Resonance and Optical Spectroscopic Evidence for Interaction between Siroheme and Fe4S4 Prosthetic Groups in Escherichia coli Sulfite Reductase Hemoprotein Subunit","volume":"21","author":"Janick","year":"1982","journal-title":"Biochemistry"},{"issue":"2","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1015","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1128\/jb.115.2.529-542.1973","article-title":"Isolation of Assimilatroy- and Dissimilatory-Type Sulfite Reductases from Desulfovibrio vulgaris","volume":"115","author":"Lee","year":"1973","journal-title":"J.\u00a0Bacteriol."},{"issue":"4","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1020","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1021\/ja00212a013","article-title":"Characterization of Two Dissimilatory Sulfite Reductases (Desulforubidin and Desulfoviridin) from the Sulfate-Reducing Bacteria. 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Co"},{"issue":"18","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1045","doi-asserted-by":"crossref","first-page":"11147","DOI":"10.1016\/S0021-9258(17)44398-5","article-title":"Mossbauer Evidence for Exchange-Coupled Siroheme and [4Fe-4S] Prosthetic Groups in Escherichia coli Sulfite Reductase. Studies of the Reduced States and of a Nitrite Turnover Complex","volume":"258","author":"Christner","year":"1983","journal-title":"J.\u00a0Biol. Chem."},{"issue":"22","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1050","doi-asserted-by":"crossref","first-page":"6786","DOI":"10.1021\/ja00334a054","article-title":"Exchange Coupling between Siroheme and Iron-Sulfur ([4Fe-4S]) Cluster in E.\u00a0coli Sulfite Reductase. Moessbauer Studies and Coupling Models for a 2-Electron Reduced Enzyme State and Complexes with Sulfide","volume":"106","author":"Christner","year":"1984","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"24","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1055","doi-asserted-by":"crossref","first-page":"15373","DOI":"10.1016\/S0021-9258(17)42559-2","article-title":"Characterization of a Sulfite Reductase from Desulfovibrio vulgaris. Evidence for the Presence of a Low-Spin Siroheme and an Exchange-Coupled Siroheme-[4Fe-4S] Unit","volume":"259","author":"Huynh","year":"1984","journal-title":"J.\u00a0Biol. Chem."},{"issue":"26","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1060","doi-asserted-by":"crossref","first-page":"6976","DOI":"10.1021\/ja00131a021","article-title":"Double Exchange and Vibronic Coupling in Mixed-Valence Systems. Electronic Structure of Exchange-Coupled Siroheme-[Fe4S4]2+ Chromophore in Oxidized E.\u00a0coli Sulfite Reductase","volume":"117","author":"Bominaar","year":"1995","journal-title":"J.\u00a0Am. Chem. 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Biol."},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib1090","doi-asserted-by":"crossref","first-page":"71","DOI":"10.3389\/fmicb.2011.00071","article-title":"Structural Insights into Dissimilatory Sulfite Reductases: Structure of Desulforubidin from Desulfomicrobium norvegicum","volume":"2","author":"Oliveira","year":"2011","journal-title":"Front. Microbiol."},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1095","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1111\/j.1365-2958.2010.07390.x","article-title":"Structural Insights into the Enzyme Catalysis from Comparison of Three Forms of Dissimilatory Sulphite Reductase from Desulfovibrio gigas","volume":"78","author":"Hsieh","year":"2010","journal-title":"Mol. 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Biochem."},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1115","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1021\/ar960260e","article-title":"Role of Nucleotides in Nitrogenase Catalysis","volume":"30","author":"Seefeldt","year":"1997","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib1120","series-title":"Advances in Inorganic Chemistry","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0898-8838(08)60078-1","article-title":"Structure, Function, and Biosynthesis of the Metallosulfur Clusters in Nitrogenases","volume":"vol. 47","author":"Smith","year":"1999"},{"issue":"12","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1125","doi-asserted-by":"crossref","first-page":"4969","DOI":"10.1021\/acs.chemrev.0c00067","article-title":"Structural Enzymology of Nitrogenase Enzymes","volume":"120","author":"Einsle","year":"2020","journal-title":"Chem. Rev."},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib1130","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-1-61779-194-9_1","article-title":"Historic Overview of Nitrogenase Research","volume":"766","author":"Hu","year":"2011","journal-title":"Methods Mol. Biol."},{"issue":"12","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1135","doi-asserted-by":"crossref","first-page":"5082","DOI":"10.1021\/acs.chemrev.9b00556","article-title":"Reduction of Substrates by Nitrogenases","volume":"120","author":"Seefeldt","year":"2020","journal-title":"Chem. Rev."},{"issue":"2","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1140","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1021\/ar300267m","article-title":"Nitrogenase: A Draft Mechanism","volume":"46","author":"Hoffman","year":"2013","journal-title":"Acc. Chem. Res."},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1145","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1007\/s00775-014-1116-7","article-title":"Nitrogenase FeMo Cofactor: An Atomic Structure in Three Simple Steps","volume":"19","author":"Einsle","year":"2014","journal-title":"J.\u00a0Biol. Inorg. Chem."},{"issue":"9","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1150","doi-asserted-by":"crossref","first-page":"956","DOI":"10.1038\/nchembio.2428","article-title":"The Structure of Vanadium Nitrogenase Reveals an Unusual Bridging Ligand","volume":"13","author":"Sippel","year":"2017","journal-title":"Nat. Chem. Biol."},{"issue":"7","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1155","doi-asserted-by":"crossref","first-page":"3013","DOI":"10.1021\/cr950057h","article-title":"Structure-Function Relationships of Alternative Nitrogenases","volume":"96","author":"Eady","year":"1996","journal-title":"Chem. 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A."},{"issue":"8","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1345","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1007\/s00775-009-0572-y","article-title":"Immobilization of the hyperthermophilic hydrogenase from Aquifex aeolicus bacterium onto gold and carbon nanotube electrodes for efficient H2 oxidation","volume":"14","author":"Luo","year":"2009","journal-title":"J.\u00a0Biol. Inorg. Chem."},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1350","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1038\/nchembio.1500","article-title":"Reversible [4Fe-3S] Cluster Morphing in an O(2)-Tolerant [NiFe] Hydrogenase","volume":"10","author":"Frielingsdorf","year":"2014","journal-title":"Nat. Chem. Biol."},{"issue":"1","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1355","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.str.2012.11.010","article-title":"Crystal Structure of the O(2)-Tolerant Membrane-Bound Hydrogenase 1 from Escherichia coli in Complex with its Cognate Cytochrome b","volume":"21","author":"Volbeda","year":"2013","journal-title":"Structure"},{"issue":"24","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1360","doi-asserted-by":"crossref","first-page":"8512","DOI":"10.1021\/ja503138p","article-title":"Enhanced Oxygen-Tolerance of the Full Heterotrimeric Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha","volume":"136","author":"Radu","year":"2014","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1365","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1002\/cphc.200901002","article-title":"H2 Conversion in the Presence of O2 as Performed by the Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha","volume":"11","author":"Lenz","year":"2010","journal-title":"Chemphyschem"},{"issue":"1","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1370","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1111\/j.1432-1033.1992.tb17297.x","article-title":"Further Characterization of the [Fe]-Hydrogenase from Desulfovibrio desulfuricans ATCC 7757","volume":"209","author":"Hatchikian","year":"1992","journal-title":"Eur. J. Biochem."},{"issue":"1","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1375","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/0014-5793(78)80112-4","article-title":"Separation of Hydrogenase from Intact Cells of Desulfovibrio vulgaris. 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Chem. Soc."},{"issue":"40","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1425","doi-asserted-by":"crossref","first-page":"12969","DOI":"10.1021\/bi9913193","article-title":"Binding of Exogenously Added Carbon Monoxide at the Active Site of the Iron-Only Hydrogenase (CpI) from Clostridium pasteurianum","volume":"38","author":"Lemon","year":"1999","journal-title":"Biochemistry"},{"issue":"15","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1430","doi-asserted-by":"crossref","first-page":"3793","DOI":"10.1021\/ja9943703","article-title":"Photochemistry at the Active Site of the Carbon Monoxide Inhibited Form of the Iron-Only Hydrogenase (CpI)","volume":"122","author":"Lemon","year":"2000","journal-title":"J.\u00a0Am. Chem. 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Res."},{"issue":"12","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1630","doi-asserted-by":"crossref","first-page":"3342","DOI":"10.1039\/C8EE02361A","article-title":"Direct Visible Light Activation of a Surface Cysteine-Engineered [NiFe]-Hydrogenase by Silver Nanoclusters","volume":"11","author":"Zhang","year":"2018","journal-title":"Energ. Environ. 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Biol."},{"issue":"7","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1655","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1002\/ejic.201001127","article-title":"Nickel\u2013iron\u2013selenium hydrogenases \u2013 An overview","volume":"2011","author":"Baltazar","year":"2011","journal-title":"Eur. J. Inorg. Chem."},{"issue":"2","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1660","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1432-1033.1990.tb15499.x","article-title":"The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mossbauer Characterization","volume":"189","author":"Teixeira","year":"1990","journal-title":"Eur. J. Biochem."},{"issue":"40","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1665","doi-asserted-by":"crossref","first-page":"13410","DOI":"10.1021\/ja803657d","article-title":"The Difference a se Makes? Oxygen-Tolerant Hydrogen Production by the [NiFeSe]-Hydrogenase from Desulfomicrobium baculatum","volume":"130","author":"Parkin","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"7-8","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1670","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1002\/elan.200880002","article-title":"Enzymatic Anodes for Hydrogen Fuel Cells Based on Covalent Attachment of Ni-Fe Hydrogenases and Direct Electron Transfer to SAM-Modified Gold Electrodes","volume":"22","author":"R\u00fcdiger","year":"2010","journal-title":"Electroanalysis"},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1675","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1007\/s00775-005-0022-4","article-title":"Hydrogenases in Desulfovibrio Vulgaris Hildenborough: Structural and Physiologic Characterisation of the Membrane-Bound [NiFeSe] Hydrogenase","volume":"10","author":"Valente","year":"2005","journal-title":"J.\u00a0Biol. Inorg. 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Microbiol."},{"issue":"7","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1725","doi-asserted-by":"crossref","first-page":"2515","DOI":"10.1021\/cr950058+","article-title":"Nickel-Containing Carbon Monoxide Dehydrogenase\/Acetyl-CoA Synthase","volume":"96","author":"Ragsdale","year":"1996","journal-title":"Chem. Rev."},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1730","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/S0959-440X(98)80095-X","article-title":"Active Sites of Transition-Metal Enzymes with a Focus on Nickel","volume":"8","author":"Ermler","year":"1998","journal-title":"Curr. Opin. Struct. Biol."},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1735","doi-asserted-by":"crossref","first-page":"E1166","DOI":"10.1073\/pnas.1716667115","article-title":"Evolutionary History of Carbon Monoxide Dehydrogenase\/Acetyl-CoA Synthase, One of the Oldest Enzymatic Complexes","volume":"115","author":"Adam","year":"2018","journal-title":"Proc. Natl. 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Rev."},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1780","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1021\/bi011586k","article-title":"Spectroscopic Studies of Nickel-Deficient Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum: Nature of the Iron-Sulfur Clusters","volume":"41","author":"Craft","year":"2002","journal-title":"Biochemistry"},{"issue":"29","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1785","doi-asserted-by":"crossref","first-page":"8702","DOI":"10.1021\/bi00195a011","article-title":"Organization of Clusters and Internal Electron Pathways in CO Dehydrogenase from Clostridium thermoaceticum: Relevance to the Mechanism of Catalysis and Cyanide Inhibition","volume":"33","author":"Anderson","year":"1994","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1790","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/nsb912","article-title":"Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] Clusters in Closed and Open Subunits of Acetyl-CoA Synthase\/Carbon Monoxide Dehydrogenase","volume":"10","author":"Darnault","year":"2003","journal-title":"Nat. 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Sci."},{"issue":"5593","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1810","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1126\/science.1075843","article-title":"A\u00a0Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase\/Acetyl-CoA Synthase","volume":"298","author":"Doukov","year":"2002","journal-title":"Science"},{"issue":"8","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1815","doi-asserted-by":"crossref","first-page":"6101","DOI":"10.1074\/jbc.M210484200","article-title":"Nickel in Subunit Beta of the Acetyl-CoA Decarbonylase\/Synthase Multienzyme Complex in Methanogens. Catalytic Properties and Evidence for a Binuclear Ni-Ni Site","volume":"278","author":"Gencic","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1820","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1002\/pro.3836","article-title":"Structure, Function, and Biosynthesis of Nickel-Dependent Enzymes","volume":"29","author":"Alfano","year":"2020","journal-title":"Protein Sci."},{"issue":"4","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1825","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1007\/s00775-018-1541-0","article-title":"Maturation of the [Ni-4Fe-4S] Active Site of Carbon Monoxide Dehydrogenases","volume":"23","author":"Merrouch","year":"2018","journal-title":"J.\u00a0Biol. Inorg. Chem."},{"issue":"7","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1830","doi-asserted-by":"crossref","first-page":"3873","DOI":"10.1016\/S0021-9258(19)39675-9","article-title":"CO Dehydrogenase from Clostridium Thermoaceticum. 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Soc."},{"issue":"4","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1845","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1021\/ja9528386","article-title":"Nature of the C-Cluster in Ni-Containing Carbon Monoxide Dehydrogenases","volume":"118","author":"Hu","year":"1996","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"48","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1850","doi-asserted-by":"crossref","first-page":"15697","DOI":"10.1021\/bi990397n","article-title":"Stoichiometric CO Reductive Titrations of Acetyl-CoA Synthase (Carbon Monoxide Dehydrogenase) from Clostridium thermoaceticum","volume":"38","author":"Fraser","year":"1999","journal-title":"Biochemistry"},{"issue":"28","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1855","doi-asserted-by":"crossref","first-page":"10016","DOI":"10.1021\/bi980149b","article-title":"CO\/CO2 Potentiometric Titrations of Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum and the Effect of CO2","volume":"37","author":"Russell","year":"1998","journal-title":"Biochemistry"},{"issue":"48","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1860","doi-asserted-by":"crossref","first-page":"15706","DOI":"10.1021\/bi990398f","article-title":"Evidence for a Proposed Intermediate Redox State in the CO\/CO(2) Active Site of Acetyl-CoA Synthase (Carbon Monoxide Dehydrogenase) from Clostridium thermoaceticum","volume":"38","author":"Fraser","year":"1999","journal-title":"Biochemistry"},{"issue":"7","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1865","doi-asserted-by":"crossref","first-page":"3880","DOI":"10.1016\/S0021-9258(19)39676-0","article-title":"Mossbauer Study of CO Dehydrogenase from Clostridium thermoaceticum","volume":"265","author":"Lindahl","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"issue":"24","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1870","doi-asserted-by":"crossref","first-page":"7879","DOI":"10.1021\/bi00024a012","article-title":"Mechanism of CO Oxidation by Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum and its Inhibition by Anions","volume":"34","author":"Seravalli","year":"1995","journal-title":"Biochemistry"},{"issue":"29","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1875","doi-asserted-by":"crossref","first-page":"8560","DOI":"10.1002\/anie.201501778","article-title":"How the [NiFe4S4] Cluster of CO Dehydrogenase Activates CO2 and NCO(\u2212)","volume":"54","author":"Fesseler","year":"2015","journal-title":"Angew. Chem. Int. Ed. Engl."},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1880","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1021\/ic102304m","article-title":"Carbon Monoxide Dehydrogenase Reaction Mechanism: A Likely Case of Abnormal CO2 Insertion to a Ni-H(\u2212) Bond","volume":"50","author":"Amara","year":"2011","journal-title":"Inorg. Chem."},{"issue":"1","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1885","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.jinorgbio.2011.08.012","article-title":"Metal-Metal Bonds in Biology","volume":"106","author":"Lindahl","year":"2012","journal-title":"J.\u00a0Inorg. Biochem."},{"issue":"43","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1890","doi-asserted-by":"crossref","first-page":"13690","DOI":"10.1021\/acs.jpcb.5b03098","article-title":"Investigations by Protein Film Electrochemistry of Alternative Reactions of Nickel-Containing Carbon Monoxide Dehydrogenase","volume":"119","author":"Wang","year":"2015","journal-title":"J.\u00a0Phys. Chem. B"},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1895","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1039\/C5SC04554A","article-title":"When the Inhibitor Tells More than the Substrate: The Cyanide-Bound State of a Carbon Monoxide Dehydrogenase","volume":"7","author":"Ciaccafava","year":"2016","journal-title":"Chem. Sci."},{"issue":"26","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1900","doi-asserted-by":"crossref","first-page":"7398","DOI":"10.1002\/anie.201703225","article-title":"Carbon monoxide dehydrogenase reduces cyanate to cyanide","volume":"56","author":"Ciaccafava","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"issue":"48","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1905","doi-asserted-by":"crossref","first-page":"15466","DOI":"10.1002\/anie.201709261","article-title":"CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2","volume":"56","author":"Domnik","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"issue":"20","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1910","doi-asserted-by":"crossref","first-page":"6811","DOI":"10.1073\/pnas.82.20.6811","article-title":"Evidence that an Iron-Nickel-Carbon Complex Is Formed by Reaction of CO with the CO Dehydrogenase from Clostridium thermoaceticum","volume":"82","author":"Ragsdale","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"24","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1915","doi-asserted-by":"crossref","first-page":"6489","DOI":"10.1021\/ja00129a011","article-title":"Nickel-Mediated Formation of Thio Esters from Bound Methyl, Thiols, and Carbon Monoxide: A Possible Reaction Pathway of Acetyl-Coenzyme a Synthase Activity in Nickel-Containing Carbon Monoxide Dehydrogenases","volume":"117","author":"Tucci","year":"1995","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"2","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1920","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1021\/bi00216a018","article-title":"Characterization of the Ni-Fe-C Complex Formed by Reaction of Carbon Monoxide with the Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum by Q-Band ENDOR","volume":"30","author":"Fan","year":"1991","journal-title":"Biochemistry"},{"issue":"35","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1925","doi-asserted-by":"crossref","first-page":"8301","DOI":"10.1021\/ja971025+","article-title":"M\u00f6ssbauer and EPR Study of the Ni-Activated \u03b1-Subunit of Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum","volume":"119","author":"Xia","year":"1997","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"30","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1930","doi-asserted-by":"crossref","first-page":"7502","DOI":"10.1021\/ja981165z","article-title":"Spectroscopic, Redox, and Structural Characterization of the Ni-Labile and Nonlabile Forms of the Acetyl-CoA Synthase Active. Site of Carbon Monoxide Dehydrogenase","volume":"120","author":"Russell","year":"1998","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"13","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1935","doi-asserted-by":"crossref","first-page":"5522","DOI":"10.1021\/ja00066a021","article-title":"Heterogeneous Nickel-Iron Environments in Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum","volume":"115","author":"Shin","year":"1993","journal-title":"J.\u00a0Am. Chem. 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Chem."},{"issue":"3","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1950","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1016\/0304-4165(65)90205-9","article-title":"S-Adenosyl-L-Methionine, a Component of the Clastic Dissimilation of Pyruvate in Escherichia coli","volume":"107","author":"Knappe","year":"1965","journal-title":"Biochim. Biophys. Acta"},{"issue":"7","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1955","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.1016\/S0021-9258(19)77160-9","article-title":"Lysine 2,3-Aminomutase. Purification and Properties of a Pyridoxal Phosphate and S-Adenosylmethionine-Activated Enzyme","volume":"245","author":"Chirpich","year":"1970","journal-title":"J.\u00a0Biol. 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Biol."},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1965","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1093\/nar\/29.5.1097","article-title":"Radical SAM, a Novel Protein Superfamily Linking Unresolved Steps in Familiar Biosynthetic Pathways with Radical Mechanisms: Functional Characterization Using New Analysis and Information Visualization Methods","volume":"29","author":"Sofia","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib1970","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.mie.2018.06.004","article-title":"Atlas of the Radical SAM Superfamily: Divergent Evolution of Function Using a \u201cPlug and Play\u201d Domain","volume":"606","author":"Holliday","year":"2018","journal-title":"Methods Enzymol."},{"issue":"8","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1975","doi-asserted-by":"crossref","first-page":"4229","DOI":"10.1021\/cr4004709","article-title":"Radical S-Adenosylmethionine Enzymes","volume":"114","author":"Broderick","year":"2014","journal-title":"Chem. 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Virol."},{"issue":"5896","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1985","doi-asserted-by":"crossref","first-page":"1670","DOI":"10.1126\/science.1160446","article-title":"An Alternative Menaquinone Biosynthetic Pathway Operating in Microorganisms","volume":"321","author":"Hiratsuka","year":"2008","journal-title":"Science"},{"issue":"40","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1990","doi-asserted-by":"crossref","first-page":"5229","DOI":"10.1021\/acs.biochem.7b00771","article-title":"Radical S-Adenosylmethionine Enzymes Involved in RiPP Biosynthesis","volume":"56","author":"Mahanta","year":"2017","journal-title":"Biochemistry"},{"issue":"45","key":"10.1016\/B978-0-12-823144-9.00116-3_bib1995","doi-asserted-by":"crossref","first-page":"6072","DOI":"10.1021\/acs.biochem.7b01056","article-title":"Correction to Radical S-Adenosylmethionine Enzymes Involved in RiPP Biosynthesis","volume":"56","author":"Mahanta","year":"2017","journal-title":"Biochemistry"},{"issue":"1","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2000","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.abb.2004.10.003","article-title":"The Novel Structure and Chemistry of Iron-Sulfur Clusters in the Adenosylmethionine-Dependent Radical Enzyme Biotin Synthase","volume":"433","author":"Jarrett","year":"2005","journal-title":"Arch. 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Chem."},{"issue":"31","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2070","doi-asserted-by":"crossref","first-page":"9584","DOI":"10.1021\/bi060840b","article-title":"4-Hydroxyphenylacetate Decarboxylases: Properties of a Novel Subclass of Glycyl Radical Enzyme Systems","volume":"45","author":"Yu","year":"2006","journal-title":"Biochemistry"},{"issue":"15","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2075","doi-asserted-by":"crossref","first-page":"14570","DOI":"10.1074\/jbc.M313855200","article-title":"Post-Translational Formylglycine Modification of Bacterial Sulfatases by the Radical S-Adenosylmethionine Protein AtsB","volume":"279","author":"Fang","year":"2004","journal-title":"J.\u00a0Biol. 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Chem."},{"issue":"21","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2220","doi-asserted-by":"crossref","first-page":"15669","DOI":"10.1074\/jbc.275.21.15669","article-title":"The Activating Component of the Anaerobic Ribonucleotide Reductase from Escherichia coli. An Iron-Sulfur Center with Only Three Cysteines","volume":"275","author":"Tamarit","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"issue":"1","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2225","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/S0003-9861(02)00421-6","article-title":"Electron Acceptor Specificity of Ferredoxin (Flavodoxin):NADP+ Oxidoreductase from Escherichia coli","volume":"406","author":"Wan","year":"2002","journal-title":"Arch. Biochem. Biophys."},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2230","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1039\/b703109m","article-title":"Iron-Sulfur Proteins as Initiators of Radical Chemistry","volume":"24","author":"Marquet","year":"2007","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib2235","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/bs.mie.2018.06.002","article-title":"Determining Redox Potentials of the Iron-Sulfur Clusters of the AdoMet Radical Enzyme Superfamily","volume":"606","author":"Maiocco","year":"2018","journal-title":"Methods Enzymol."},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib2240","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.cbpa.2020.01.007","article-title":"Adenosylation Reactions Catalyzed by the Radical S-Adenosylmethionine Superfamily Enzymes","volume":"55","author":"Ding","year":"2020","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"12","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2245","doi-asserted-by":"crossref","first-page":"7651","DOI":"10.1016\/S0021-9258(20)89497-6","article-title":"Molecular Properties of Lysine-2,3-Aminomutase","volume":"266","author":"Song","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"issue":"39","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2250","doi-asserted-by":"crossref","first-page":"13819","DOI":"10.1073\/pnas.0505726102","article-title":"The X-Ray Crystal Structure of Lysine-2,3-Aminomutase from Clostridium subterminale","volume":"102","author":"Lepore","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"6","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2255","doi-asserted-by":"crossref","first-page":"2129","DOI":"10.1021\/cr020422m","article-title":"S-Adenosylmethionine: A Wolf in sheep\u2019s Clothing, or a Rich man\u2019s Adenosylcobalamin?","volume":"103","author":"Frey","year":"2003","journal-title":"Chem. Rev."},{"issue":"8","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2260","doi-asserted-by":"crossref","first-page":"2578","DOI":"10.1021\/bi972417w","article-title":"S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-Aminomutase and Observation of the Catalytically Functional Iron-Sulfur Centers by Electron Paramagnetic Resonance","volume":"37","author":"Lieder","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib2265","first-page":"1","article-title":"Lysine 2,3-Aminomutase and the Mechanism of the Interconversion of Lysine and Beta-Lysine","volume":"66","author":"Frey","year":"1993","journal-title":"Adv. Enzymol. Relat. Areas Mol. Biol."},{"issue":"31","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2270","doi-asserted-by":"crossref","first-page":"14859","DOI":"10.1016\/S0021-9258(18)48103-3","article-title":"The Role of S-Adenosylmethionine in the Lysine 2,3-Aminomutase Reaction","volume":"262","author":"Moss","year":"1987","journal-title":"J.\u00a0Biol. Chem."},{"issue":"22","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2275","doi-asserted-by":"crossref","first-page":"7111","DOI":"10.1021\/jacs.5b00498","article-title":"Why Nature Uses Radical SAM Enzymes So Widely: Electron Nuclear Double Resonance Studies of Lysine 2,3-Aminomutase Show the 5\u2032-dAdo\u2217 \u201cFree Radical\u201d Is Never Free","volume":"137","author":"Horitani","year":"2015","journal-title":"J.\u00a0Am. Chem. 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Biol."},{"issue":"6361","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2310","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1126\/science.aan4574","article-title":"Destruction and Reformation of an Iron-Sulfur Cluster during Catalysis by Lipoyl Synthase","volume":"358","author":"McCarthy","year":"2017","journal-title":"Science"},{"issue":"5","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2315","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1073\/pnas.81.5.1332","article-title":"Post-Translational Activation Introduces a Free Radical into Pyruvate Formate-Lyase","volume":"81","author":"Knappe","year":"1984","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"10","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2320","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1038\/13341","article-title":"Structure and Mechanism of the Glycyl Radical Enzyme Pyruvate Formate-Lyase","volume":"6","author":"Becker","year":"1999","journal-title":"Nat. Struct. Biol."},{"issue":"31","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2325","doi-asserted-by":"crossref","first-page":"7396","DOI":"10.1021\/ja9711425","article-title":"Pyruvate Formate-Lyase Activating Enzyme Is an Iron-Sulfur Protein","volume":"119","author":"Broderick","year":"1997","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"17","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2330","doi-asserted-by":"crossref","first-page":"12432","DOI":"10.1016\/S0021-9258(18)99892-3","article-title":"Adenosylmethionine-Dependent Synthesis of the Glycyl Radical in Pyruvate Formate-Lyase by Abstraction of the Glycine C-2 pro-S Hydrogen-Atom - Studies of [H-2]Glycine-Substituted Enzyme and Peptides Homologous to the Glycine-734 Site","volume":"269","author":"Frey","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"issue":"3","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2335","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1111\/j.1432-1033.1982.tb06569.x","article-title":"Routes of Flavodoxin and Ferredoxin Reduction in Escherichia coli. CoA-Acylating Pyruvate: Flavodoxin and NADPH: Flavodoxin Oxidoreductases Participating in the Activation of Pyruvate Formate-Lyase","volume":"123","author":"Blaschkowski","year":"1982","journal-title":"Eur. J. Biochem."},{"issue":"34","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2340","doi-asserted-by":"crossref","first-page":"8331","DOI":"10.1021\/ja002012q","article-title":"The [4Fe-4S](1+) Cluster of Pyruvate Formate-Lyase Activating Enzyme Generates the Glycyl Radical on Pyruvate Formate-Lyase: EPR-Detected Single Turnover","volume":"122","author":"Henshaw","year":"2000","journal-title":"J.\u00a0Am. Chem. 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A."},{"issue":"3","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2815","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1073\/pnas.0913045107","article-title":"Probing the Reaction Mechanism of IspH Protein by X-Ray Structure Analysis","volume":"107","author":"Grawert","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"51","key":"10.1016\/B978-0-12-823144-9.00116-3_bib2820","doi-asserted-by":"crossref","first-page":"17206","DOI":"10.1021\/ja806668q","article-title":"Structure of (E)-4-Hydroxy-3-Methyl-but-2-Enyl Diphosphate Reductase, the Terminal Enzyme of the Non-mevalonate Pathway","volume":"130","author":"Rekittke","year":"2008","journal-title":"J.\u00a0Am. Chem. 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Dis."},{"issue":"2","key":"10.1016\/B978-0-12-823144-9.00116-3_bib3150","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1038\/sj.emboj.7600041","article-title":"Genetic Ablations of Iron Regulatory Proteins 1 and 2 Reveal why Iron Regulatory Protein 2 Dominates Iron Homeostasis","volume":"23","author":"Meyron-Holtz","year":"2004","journal-title":"EMBO J."},{"key":"10.1016\/B978-0-12-823144-9.00116-3_bib3155","doi-asserted-by":"crossref","first-page":"124","DOI":"10.3389\/fphar.2014.00124","article-title":"The Physiological Functions of Iron Regulatory Proteins in Iron Homeostasis - An Update","volume":"5","author":"Zhang","year":"2014","journal-title":"Front. 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