Structural insight into the high reduction potentials observed for Fusobacterium nucleatum flavodoxin.

ABSTRACT: Flavodoxins are small flavin mononucleotide (FMN)-containing proteins that mediate a variety of electron transfer processes. The primary sequence of flavodoxin from Fusobacterium nucleatum, a pathogenic oral bacterium, is marked with a number of distinct features including a glycine to lysine (K13) substitution in the highly conserved phosphate-binding loop (T/S-X-T-G-X-T), variation in the aromatic residues that sandwich the FMN cofactor, and a more even distribution of acidic and basic residues. The E_ox/sq (oxidized/semiquinone; -43 mV) and E_sq/hq (semiquinone/hydroquinone; -256 mV) are the highest recorded reduction potentials of known long-chain flavodoxins. These more electropositive values are a consequence of the apoprotein binding to the FMN hydroquinone anion

SUBMITTER: Mothersole RG 

PROVIDER: S-EPMC6635775 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature