molybdopterin-guanine-dinucleotide and ferrous-sulfide

molybdopterin-guanine-dinucleotide has been researched along with ferrous-sulfide* in 1 studies

Other Studies

1 other study(ies) available for molybdopterin-guanine-dinucleotide and ferrous-sulfide

Article	Year
Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science (New York, N.Y.), 1997, Feb-28, Volume: 275, Issue:5304 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. Topics: Binding Sites; Carbon Dioxide; Catalysis; Crystallography, X-Ray; Electron Transport; Escherichia coli; Ferrous Compounds; Formate Dehydrogenases; Formates; Guanine Nucleotides; Hydrogen Bonding; Hydrogenase; Ligands; Models, Molecular; Molecular Sequence Data; Molybdenum; Multienzyme Complexes; Nitrites; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Pterins; Selenocysteine	1997

Article

Year

Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster.

Science (New York, N.Y.), 1997, Feb-28, Volume: 275, Issue:5304

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.

Topics: Binding Sites; Carbon Dioxide; Catalysis; Crystallography, X-Ray; Electron Transport; Escherichia coli; Ferrous Compounds; Formate Dehydrogenases; Formates; Guanine Nucleotides; Hydrogen Bonding; Hydrogenase; Ligands; Models, Molecular; Molecular Sequence Data; Molybdenum; Multienzyme Complexes; Nitrites; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Pterins; Selenocysteine

1997