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

机译:黄素蛋白的结构和机理方面:电子通过一氧化氮合酶黄素蛋白结构域转移

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摘要

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.
机译:一氧化氮合酶属于双黄素酶家族,可将电子从NAD(P)H转移至各种血红素蛋白受体。在催化过程中,它们的FMN子域通过充当电子受体(从FAD接收电子)和电子供体而发挥中心作用,并被认为会经历大的构象运动并在此过程中参与两种不同的蛋白质-蛋白质相互作用。这篇小型综述总结了我们对调节一氧化氮合酶黄素蛋白结构域功能的许多因素的了解,主要是从它们如何影响电子输入/输出和FMN子结构域的构象行为的角度出发。

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