Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain

Authors


D. J. Stuehr, Department of Pathobiology, Lerner Research Institute (NC22), The Cleveland Clinic, 9500 Euclid Ave, Cleveland, OH 44195, USA
Fax: 1 216 636 0104
Tel: +1 216 445 6950
E-mail: stuehrd@ccf.org

Abstract

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.

Ancillary