Formate dehydrogenase (acceptor) (EC 1.1.99.33, FDHH, FDH-H, FDH-O, formate dehydrogenase H, formate dehydrogenase O) is an enzyme with systematic name formate:acceptor oxidoreductase. [1][2][3] This enzyme catalyses the following chemical reaction.

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Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD + in formate:NAD+ oxidoreductase (EC 1.17.1.9) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1). [1] .

Formate de­hydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions.

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2024年7月24日 · Formate dehydrogenases (FDHs) are widely utilized to drive various biocatalysts for the production of valuable compounds. Recent advancements in enzyme engineering have enhanced the functionality of metal-independent FDHs, increasing their applicability and suitability for specific bioprocesses.

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Escherichia coli synthesizes a hydrogenase-linked formate dehydrogenase (FDHH) under anaerobic conditions in the absence of nitrate.

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Four classes of Escherichia coli mutants deficient in either or both of their anaerobic selenium-containing formate dehydrogenases (FDH) were isolated. A class I mutant devoid of FDHH activity specifically linked to benzyl viologen (BV) produced a small amount of the FDHH 80,000 dalton selenopeptide.