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Two important biological reaction mechanisms of nitric oxide are S- nitrosation of thiols, and nitrosylation of transition metal ions. S-nitrosation involves the (reversible) conversion of thiol groups, including cysteine residues in proteins, to form S-nitrosothiols (RSNOs). S- Nitrosation is a mechanism for dynamic, post-translational regulation of most or all major classes of protein. [55] The second mechanism, nitrosylation, involves the binding of ·NO to a transition metal ion like iron or copper. In this function, ·NO is referred to as a nitrosyl ligand. Typical cases involve the nitrosylation of heme proteins like cytochromes, thereby disabling the normal enzymatic activity of the enzyme. Nitrosylated ferrous iron is particularly stable, as the binding of the nitrosyl ligand to ferrous iron (Fe(II)) is very strong. Hemoglobin is a prominent example of a heme protein that may be modified by ·NO by both pathways: ·NO may attach directly to the heme in the nitrosylation reaction, and independently form S-nitrosothiols by S-nitrosation of the thiol moieties. [56]

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Testo extreme anabolic forum

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