Premium
The redox switch: dynamic regulation of protein function by cysteine modifications
Author(s) -
Spadaro Davide,
Yun ByungWook,
Spoel Steven H.,
Chu Chengcai,
Wang YiQin,
Loake Gary J.
Publication year - 2010
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.2009.01307.x
Subject(s) - cysteine , redox , chemistry , reactive nitrogen species , s nitrosylation , nitric oxide , biochemistry , nitrosylation , hydrogen peroxide , function (biology) , hypochlorous acid , reactive oxygen species , cysteine metabolism , sulfenic acid , enzyme , microbiology and biotechnology , biology , organic chemistry
Reactive oxygen intermediates (ROIs) and reactive nitrogen intermediates (RNIs) have now become well established as important signalling molecules in physiological settings within microorganisms, mammals and plants. These intermediates are routinely synthesised in a highly controlled and transient fashion by NADPH‐dependent enzymes, which constitute key regulators of redox signalling. Mild oxidants such as hydrogen peroxide (H 2 O 2 ) and especially nitric oxide (NO) signal through chemical reactions with specific atoms of target proteins that result in covalent protein modifications. Specifically, highly reactive cysteine (Cys) residues of low pK a are a major site of action for these intermediates. The oxidation of target Cys residues can result in a number of distinct redox‐based, post‐translational modifications including S‐nitrosylation, S‐glutathionylation; and sulphenic acid, sulphinic acid and disulphide formation. Importantly, such modifications precisely regulate protein structure and function. Cys‐based redox switches are now increasingly being found to underpin many different signalling systems and regulate physiological outputs across kingdoms.