Control of Electron Transfer and Catalysis in Neuronal Nitric-oxide Synthase (nNOS) by a Hinge Connecting Its FMN and FAD-NADPH Domains
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Title
Control of Electron Transfer and Catalysis in Neuronal Nitric-oxide Synthase (nNOS) by a Hinge Connecting Its FMN and FAD-NADPH Domains
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 36, Pages 30105-30116
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2012-06-23
DOI
10.1074/jbc.m112.339697
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Note: Only part of the references are listed.- A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme - simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains
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- Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain
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- Neutralizing a Surface Charge on the FMN Subdomain Increases the Activity of Neuronal Nitric-oxide Synthase by Enhancing the Oxygen Reactivity of the Enzyme Heme-Nitric Oxide Complex
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- Lys842in Neuronal Nitric-oxide Synthase Enables the Autoinhibitory Insert to Antagonize Calmodulin Binding, Increase FMN Shielding, and Suppress Interflavin Electron Transfer
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