Characterization of Key Residues in the Subdomain Encoded by Exons 8 and 9 of Human Inducible Nitric Oxide Synthase: A Critical Role for Asp-280 in Substrate Binding and Subunit Interactions

Human inducible nitric oxide synthase (iNOS) is active as a dimer of two identical subunits. Each subunit has an amino-terminal oxygenase domain that binds the substrate L-Arg and the cofactors heme and tetrahydrobiopterin and a carboxyl-terminal reductase domain that binds FMN, FAD, and NADPH. We p...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2001-08, Vol.98 (18), p.10392-10397
Hauptverfasser: Ghosh, Dipak K., Rashid, Mohammad B., Crane, Brian, Taskar, Varsha, Mast, Molly, Misukonis, Mary A., Weinberg, J. Brice, Eissa, N. Tony
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Sprache:eng
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