Nitric-oxide Synthase Forms N-NO-pterin and S-NO-Cys
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چکیده
منابع مشابه
Nitric-oxide Synthase Forms N-NO-pterin and S-NO-Cys
Robin J. Rosenfeld, Joseph Bonaventura**, Blair R. Szymczyna, Michael J. MacCoss, Andrew S. Arvai, John R. Yates III , John A. Tainer, and Elizabeth D. Getzoff From the Department of Molecular Biology and The Skaggs Institute for Chemical Biology, Department of Cell Biology, and Department of Chemical Physiology, The Scripps Research Institute, La Jolla, California 92037, the Department of Cell...
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Inducible nitric-oxide synthase (iNOS) produces biologically stressful levels of nitric oxide (NO) as a potent mediator of cellular cytotoxicity or signaling. Yet, how this nitrosative stress affects iNOS function in vivo is poorly understood. Here we define two specific non-heme iNOS nitrosation sites discovered by combining UV-visible spectroscopy, chemiluminescence, mass spectrometry, and x-...
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We have investigated the kinetics of NO escape from Geobacillus stearothermophilus nitric oxide synthase (gsNOS). Previous work indicated that NO release was gated at position 223 in mammalian enzymes; our kinetics experiments include mutants at that position along with measurements on the wild type enzyme. Employing stopped-flow UV-vis methods, reactions were triggered by mixing a reduced enzy...
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It has now become well accepted that nitric oxide (NO) has a key role to play in the signalling that takes place in plant cells. However, the sources of NO in plants has been hard to determine and there is considerable debate as to exactly how NO is made by plant cells. In animals nitric oxide synthase (NOS) enzymes have been characterised and such data has been used to inform the studies which...
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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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2010
ISSN: 0021-9258
DOI: 10.1074/jbc.m109.072496