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Article

Dynamic regulation of the inducible nitric-oxide synthase by NO: comparison with the endothelial isoform.

The Journal of biological chemistry - 6 Feb 2004

Gautier Clement, Négrerie Michel, Wang Zhi-Qiang, Lambry Jean-Christophe, Stuehr Dennis J, Collin Fabrice, Martin Jean-Louis, Slama-Schwok Anny

Abstract excerpt

We studied by ultrafast time-resolved absorption spectroscopy the geminate recombination of NO to the oxygenase domain of the inducible NO synthase, iNOSoxy, and to mutated proteins at position Trp-457. This tryptophan interacts with the tetrahydrobiopterin cofactor BH4, and W457A/F mutations largely reduced the catalytic formation of NO. BH4 decreases the rate of NO rebinding to the ferric iNOSoxy compared with...

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Identifiers

PMID: 14594819
DOI: 10.1074/jbc.M305048200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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