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Publication Abstract from PubMed

The ferredoxin reductase FdR9 from Thermobifida fusca, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (FNR) family, catalyses electron transfer from NADH to its physiological electron acceptor ferredoxin. It forms part of a putative three-component cytochrome P450 monooxygenase system in T. fusca comprising CYP222A1 and the [3Fe-4S]-cluster ferredoxin Fdx8 as well as FdR9. Here, FdR9 was overexpressed and purified and its crystal structure was determined at 1.9 A resolution. The overall structure of FdR9 is similar to those of other members of the FNR family and is composed of an FAD-binding domain, an NAD-binding domain and a C-terminal domain. Activity measurements with FdR9 confirmed a strong preference for NADH as the cofactor. Comparison of the FAD- and NAD-binding domains of FdR9 with those of other ferredoxin reductases revealed the presence of conserved sequence motifs in the FAD-binding domain as well as several highly conserved residues involved in FAD and NAD cofactor binding. Moreover, the NAD-binding site of FdR9 contains a modified Rossmann-fold motif, GxSxxS, instead of the classical GxGxxG motif.

Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca.,Rodriguez Buitrago JA, Klunemann T, Blankenfeldt W, Schallmey A Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):334-340. doi:, 10.1107/S2053230X2000922X. Epub 2020 Jul 28. PMID:32744244^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.