
Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
Formate dehydrogenase
Introduction
Overview
Overview
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]
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(+)
References
References
- ↑ Ferry JG (1990). “Formate dehydrogenase”. FEMS Microbiol. Rev. 7 (3–4): 377–82. PMID 2094290.
- ↑ Popov VO, Lamzin VS (1994). “NAD(+)-dependent formate dehydrogenase”. Biochem. J. 301 ( Pt 3): 625–43. PMID 8053888.
- ↑ Jormakka M, Byrne B, Iwata S (2003). “Formate dehydrogenase–a versatile enzyme in changing environments”. Curr. Opin. Struct. Biol. 13 (4): 418–23. PMID 12948771.
- ↑ Graham A, Boxer DH (1981). “The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli”. Biochem. J. 195 (3): 627–37. PMID 7032506.
- ↑ Ruiz-Herrera J, DeMoss JA (1969). “Nitrate reductase complex of Escherichia coli K-12: participation of specific formate dehydrogenase and cytochrome b1 components in nitrate reduction”. J. Bacteriol. 99 (3): 720–9. PMID 4905536.
