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Crystallographic analyses of the FdsBG subcomplex of the cytosolic formate dehydrogenase FdsDABG from Cupriavidus necator
Author(s) -
Blaha Gregor,
Young Tynan,
Niks Dimitri,
Hakopian Sheron,
Tam Timothy,
Yu Xuejun,
Hille Russ
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.02775
Subject(s) - cupriavidus necator , formate dehydrogenase , nad+ kinase , formate , chemistry , cofactor , nadh dehydrogenase , stereochemistry , dehydrogenase , biochemistry , enzyme , crystallography , biology , catalysis , bacteria , genetics , protein subunit , polyhydroxyalkanoates , gene
The soluble molybdenum‐containing, NAD + ‐dependent formate dehydrogenase FdsDABG from Cupriavidus necator belongs to the NADH dehydrogenase superfamily and catalyzes the oxidation of formate to CO 2 and the reduction of NAD + to NADH. Here, we present the first description of the crystal structure of the FdsBG subcomplex with and without bound NADH. Compared to other NADH dehydrogenases, FMN is closer to both iron‐sulfur clusters, Fe 4 S 4 in FdsB and Fe 2 S 2 in FdsG. Based on the NADH‐bound structure, we conclude that the nicotinamide ring of NADH can only access the re ‐face of FMN. However, the binding of NADH reduces the affinity of the isoalloxazine ring of FMN and allows for a conformational change of the residues that are known to undergo an oxidation state‐dependent peptide flip in canonical NADH dehydrogenases.