Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase.

ABSTRACT: Flavoproteins participate in a wide variety of physiologically relevant processes that typically involve redox reactions. Within this protein superfamily, there exists a group that is able to transfer reducing equivalents from FAD to a redox-active disulfide bridge, which further reduces disulfide bridges in target proteins to regulate their structure and function. We have identified a previously undescribed type of flavin enzyme that is exclusive to oxygenic photosynthetic prokaryotes and that is based on the primary sequence that had been assigned as an NADPH-dependent thioredoxin reductase (NTR). However, our experimental data show that the protein does not transfer reducing equivalents from flavins to disulfides as in NTRs but functions in the opposite direction. High-resolution struct

SUBMITTER: Buey RM 

PROVIDER: S-EPMC5715778 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature