Intra-subunit and Inter-subunit Electron Transfer in Neuronal Nitric-oxide Synthase
نویسندگان
چکیده
منابع مشابه
Nitric oxide synthase structure and electron transfer.
The nitric oxide synthases (NOS), although unrelated to the cytochromes P450 in terms of sequence, exhibit spectroscopic and catalytic properties strongly reminiscent of those of the P450 system. One important difference is the requirement of the NOS enzymes for tetrahydrobiopterin. The biopterin cofactor is shown by chemical studies to bind close to pyrrole ring D of the prosthetic heme group,...
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A central issue in nitric oxide (NO) research is to understand how NO can act in some settings as a servoregulator and in others as a cytotoxin. To answer this, we have sought a molecular basis for the differential regulation of the two known types of NO synthase (NOS). Constitutive NOS's in endothelium and neurons are activated by agonist-induced elevation of Ca2+ and resultant binding of calm...
متن کاملCalmodulln Is a Subunit of Nitric Oxide Synthase from Macrophages
From The Beatrice and Samuel A. Seater Laboratory, Division of Hematology-Ontology, Department of Meriting Cornell Unit~ersity Medical College, New York, New York 10021; the *Department of Biochemical and Molecular Pathology, Merck, Sharpe & Dohme Research Laboratories, Rahway, New Jersey 07065; and the *Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California ...
متن کاملCalmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer.
In neuronal nitric-oxide synthase (NOS), electron transfer proceeds across domains in a linear sequence from NADPH to flavins to heme, with calmodulin (CaM) triggering the interdomain electron transfer to the heme (Abu-Soud, H. M., and Stuehr, D. J. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 10769-10772). Here, we utilized a neuronal NOS devoid of its bound heme and tetrahydrobiopterin (apo-NOS) ...
متن کاملCalmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer.
Neuronal nitric oxide synthase (nNOS) is composed of an oxygenase domain that binds heme, (6R)-tetrahydrobiopterin, and Arg, coupled to a reductase domain that binds FAD, FMN, and NADPH. Activity requires dimeric interaction between two oxygenase domains and calmodulin binding between the reductase and oxygenase domains, which triggers electron transfer between flavin and heme groups. We constr...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m104123200