期刊
ANTIOXIDANTS
卷 10, 期 7, 页码 -出版社
MDPI
DOI: 10.3390/antiox10071111
关键词
nitrosothiol; nitric oxide; cysteine; post-translational modification; thiol
资金
- National Institute of Health [HL 086621, ES005022]
The modification of protein cysteine residues by nitric oxide is important for various biological functions. The formation of stable nitrosothiols under biologically relevant conditions is discussed in this review, with a focus on the factors influencing the selective nature of this modification. The review also explores the reaction mechanisms and the impact of sources of NO and the chemical nature of potential reaction targets.
The modification of protein cysteine residues underlies some of the diverse biological functions of nitric oxide (NO) in physiology and disease. The formation of stable nitrosothiols occurs under biologically relevant conditions and time scales. However, the factors that determine the selective nature of this modification remain poorly understood, making it difficult to predict thiol targets and thus construct informatics networks. In this review, the biological chemistry of NO will be considered within the context of nitrosothiol formation and degradation whilst considering how specificity is achieved in this important post-translational modification. Since nitrosothiol formation requires a formal one-electron oxidation, a classification of reaction mechanisms is proposed regarding which species undergoes electron abstraction: NO, thiol or S-NO radical intermediate. Relevant kinetic, thermodynamic and mechanistic considerations will be examined and the impact of sources of NO and the chemical nature of potential reaction targets is also discussed.
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