Pterin interactions with distinct reductase activities of NO synthase
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چکیده
منابع مشابه
Pterin interactions with distinct reductase activities of NO synthase.
Besides oxidizing L-arginine, neuronal NO synthase (NOS) NADPH-dependently reduces various electron acceptors, including cytochrome c and tetrazolium salts. The latter NADPH diaphorase reaction is used as a NOS-specific histochemical stain. Both reductase activities have been utilized to analyse electron transfer mechanisms within NOS. Basal L-arginine turnover by homodimeric NOS is enhanced by...
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Multidomain enzymes often rely on large conformational motions to function. However, the conformational setpoints, rates of domain motions and relationships between these parameters and catalytic activity are not well understood. To address this, we determined and compared the conformational setpoints and the rates of conformational switching between closed unreactive and open reactive states i...
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Calmodulin (CaM) activates NO synthase (NOS) by binding to a 20 amino acid interdomain hinge in the presence of Ca (2+), inducing electrons to be transferred from the FAD to the heme of the enzyme via a mobile FMN domain. The activation process is influenced by a number of structural features, including an autoinhibitory loop, the C-terminal tail of the enzyme, and a number of phosphorylation s...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2001
ISSN: 0264-6021
DOI: 10.1042/0264-6021:3560043