Although many studies have implicated nitric oxide (NO) as a key regulator for many different physiological processes in plants, less is known about how this molecule regulates these different events. As a readily diffusible free radical, NO reacts with a variety of intracellular and extracellular targets and can act as activator or inhibitor of enzymes, ion-channels or transcription factors as well as modulator of protein function. Because of its reactivity with transition metals NO can also bind to metal ions of heme groups, thereby activating soluble guanylate cyclase producing cyclic GMP. A NO-dependent cGMP signalling pathway has been proposed for plants. NO can also react with the thiol group of cysteine residues to form S -nitrosothiols ( S -nitrosylation). The majority of all NO-affected proteins seem to be regulated by S -nitrosylation making this type of protein modification a predominant mechanism in NO-signalling. Here we want to focus on this NO-dependent modification of cysteine residues, describing its chemistry/formation, specificity, and physiological function in plants.</P>
Comparative Biochemistry and Physiology - Part A: Molecular & Integrative Physiology – Elsevier
Published: Apr 1, 2007
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