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Literature summary extracted from

  • Raaijmakers, H.C.; Romao, M.J.
    Formate-reduced E. coli formate dehydrogenase H: The reinterpretation of the crystal structure suggests a new reaction mechanism (2006), J. Biol. Inorg. Chem., 11, 849-854.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.1.9 re-evaluation of crystallographic data Escherichia coli
1.17.98.4 reinterpretation of the crystal structure Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.98.4 Fe the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed Escherichia coli
1.17.98.4 Mo the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed Escherichia coli
1.17.98.4 Se the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.9 Escherichia coli P07658 isoform H
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1.17.98.4 Escherichia coli
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-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.17.1.9 formate + NAD+ = CO2 + NADH + H+ reaction mechanism: step I, formate binds directly to Mo, displacing Se-Cys140. Step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. Alternatively, step II may involve a selenium-carboxylated intermediate. Step III, electrons from MoIV are transferred via the 4Fe-4S center to an external electron acceptor and the catalytic cycle is completed Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.98.4 formate + acceptor the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed Escherichia coli CO2 + reduced acceptor
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.98.4 formate dehydrogenase H
-
 Escherichia coli