Abstract
The interaction of nitric oxide NO with proteins plays a critical role in several physiological systems extending from blood pressure regulation to neu-rotransmission 1–3 . In addition, NO produced in infected and inflamed tissue can contribute to the process of carcinogenesis 4,5 . The targets for NO on proteins are Cys and Tyr residues and bound metals such as heme-Fe2± for a recent review see ref. 6, through which NO exerts its effects by covalently modifying or oxidizing critical thiols or transition metals in proteins. Although much work has been performed in characterizing the NO-Fe2± interaction 7,8, there is considerably less data on NO-Cys interactions. One reason is the labile nature of nitrosothiols RSNOs, which are unstable in aqueous solution. It has been assumed that the lability of RSNOs is due to their propensity to undergo homolytic cleavage of the S-N bond with release of NO 9.
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Ferranti, P., Mamone, G., Malorni, A. (2000). Preparation and Mass Spectrometric Analysis of S-Nitrosohemoglobin. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:147
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DOI: https://doi.org/10.1385/1-59259-045-4:147
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