PMID:9036855
| Citation |
Boyington, JC, Gladyshev, VN, Khangulov, SV, Stadtman, TC and Sun, PD (1997) Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 275:1305-8 |
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| Abstract |
Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain alphabeta structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer. |
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| Keywords |
Binding Sites; Carbon Dioxide/metabolism; Catalysis; Crystallography, X-Ray; Electron Transport; Escherichia coli/enzymology; Ferrous Compounds/chemistry; Formate Dehydrogenases/chemistry; Formate Dehydrogenases/metabolism; Formates/metabolism; Guanine Nucleotides/chemistry; Guanine Nucleotides/metabolism; Hydrogen Bonding; Hydrogenase/chemistry; Hydrogenase/metabolism; Ligands; Models, Molecular; Molecular Sequence Data; Molybdenum/chemistry; Molybdenum/metabolism; Multienzyme Complexes/chemistry; Multienzyme Complexes/metabolism; Nitrites/chemistry; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Pterins/chemistry; Pterins/metabolism; Selenocysteine/chemistry; Selenocysteine/metabolism |
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