期刊
FEBS JOURNAL
卷 276, 期 15, 页码 3959-3974出版社
WILEY
DOI: 10.1111/j.1742-4658.2009.07120.x
关键词
conformational equilibrium; electron flux; electron transfer; flavoprotein; global kinetic model; heme protein; heme reduction; nitric oxide; protein-protein interaction; semiquinone
资金
- National Institutes of Health [GM51491, CA53914, HL76491]
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.
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