| Literature DB >> 16448092 |
Abstract
Nitric oxide (NO) plays important roles in many biological processes. S-Nitrosothiols have long been believed to have significant roles in NO biochemistry. The modified cysteine residue of hemoglobin was previously identified as a distorted S-nitrosothiol (RSNO) or an S-hydroxyamino radical (RSN*OH). Here we show that a thionitroxide (RSNHO*, S-aminyloxyl radical) is likely the observed species. Computational studies show that the thionitroxide is the only structure consistent with the electron density in the hemoglobin Cysbeta93-SNO structure previously reported. Although a metastable adduct, the thionitroxide in a hydrogen-bonding environment can form readily and release NO upon exposure to an aqueous environment. The thionitroxides could be responsible for the biological effects attributed to S-nitrosothiols or could serve as precursors to S-nitrosothiols in oxidative conditions.Entities:
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Year: 2006 PMID: 16448092 PMCID: PMC3162472 DOI: 10.1021/ja057097f
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419