Premium
Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain
Author(s) -
Stuehr Dennis J.,
Tejero Jesús,
Haque Mohammad M.
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07120.x
Subject(s) - flavoprotein , flavin group , electron transfer , chemistry , nitric oxide synthase , electron acceptor , nitric oxide , nad+ kinase , flavin adenine dinucleotide , biochemistry , enzyme , biophysics , photochemistry , cofactor , biology , organic chemistry
Nitric oxide synthases belong to a family of dual‐flavin enzymes that transfer electrons from NAD(P)H to a variety of heme protein acceptors. During catalysis, their FMN subdomain plays a central role by acting as both an electron acceptor (receiving electrons from FAD) and an electron donor, and is thought to undergo large conformational movements and engage in two distinct protein–protein interactions in the process. This minireview summarizes what we know about the many factors regulating niric oxide synthase flavoprotein domain function, primarily from the viewpoint of how they impact electron input/output and conformational behaviors of the FMN subdomain.