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- W2023254925 startingPage "3427" @default.
- W2023254925 abstract "The NO synthases (NOSs) catalyze a two-step oxidation of L-arginine (Arg) to generate nitric oxide (NO) plus L-citrulline. Because NOSs are the only hemeproteins known to contain tetrahydrobiopterin (H4B) as a bound cofactor, the function and role of H4B in their heme-based oxygen activation and catalysis is of current interest. Distinct oxidative and reductive transitions of bound H4B cofactor occur during catalysis and are associated with distinct redox transitions of the NOS heme and flavin prosthetic groups. In this perspective, we discuss the redox transitions of H4B and heme with regard to their kinetics, regulation, role in the catalytic mechanism, and how and why they may be linked." @default.
- W2023254925 created "2016-06-24" @default.
- W2023254925 creator A5025964769 @default.
- W2023254925 creator A5054358636 @default.
- W2023254925 creator A5067430639 @default.
- W2023254925 creator A5084922970 @default.
- W2023254925 date "2005-01-01" @default.
- W2023254925 modified "2023-10-14" @default.
- W2023254925 title "Exploring the redox reactions between heme and tetrahydrobiopterin in the nitric oxide synthases" @default.
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- W2023254925 doi "https://doi.org/10.1039/b506355h" @default.
- W2023254925 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16234921" @default.
- W2023254925 hasPublicationYear "2005" @default.
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