| Formate dehydrogenase N, transmembrane | |||||||||
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| Identifiers | |||||||||
| Symbol | Form-deh_trans | ||||||||
| Pfam | PF09163 | ||||||||
| InterPro | IPR015246 | ||||||||
| SCOP | 1kqf | ||||||||
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Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to bicarbonate, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.2.1.2) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1).[1]
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NAD-dependent formate dehydrogenases are important in methylotrophic yeast and bacteria and are vital in the catabolism of C1 compounds such as methanol.[2] The cytochrome-dependent enzymes are more important in anaerobic metabolism in prokaryotes.[3] For example, in E. coli, the formate:ferricytochrome-b1 oxidoreductase is an intrinsic membrane protein with two subunits and is involved in anaerobic nitrate respiration.[4][5]
NAD-dependent reaction
Formate + NAD(+) <=> CO(2) + NADH
Cytochrome-dependent reaction
Formate + 2 ferricytochrome b1 <=> CO(2) + 2 ferrocytochrome b1 + 2 H(+)
One of the enzymes in the oxidoreductase family which sometimes employ tungsten (bacterial formate dehydrogenase H) is known to use a selenium-molybdenum version of molybdopterin.[6]
The transmembrane domain of the beta subunit of formate dehydrogenase consists of a single transmembrane helix. This domain acts as a transmembrane anchor, allowing the conduction of electrons within the protein.[7]
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