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

Science. 1997 Feb 28;275(5304):1305-8. doi: 10.1126/science.275.5304.1305.

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.

MeSH terms

  • 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

Substances

  • Ferrous Compounds
  • Formates
  • Guanine Nucleotides
  • Ligands
  • Multienzyme Complexes
  • Nitrites
  • Protons
  • Pterins
  • Selenocysteine
  • formic acid
  • molybdopterin guanine dinucleotide
  • Carbon Dioxide
  • Molybdenum
  • Hydrogenase
  • Formate Dehydrogenases
  • formate hydrogenlyase
  • ferrous sulfide

Associated data

  • PIR/S18213
  • SWISSPROT/032176
  • SWISSPROT/P06131
  • SWISSPROT/P07658
  • SWISSPROT/P24183
  • SWISSPROT/P46448