Post-translational self-hydroxylation: A probe for oxygen activation mechanisms in non-heme iron enzymes

作者：Farquhar ER; Koehntop KD; Emerson JP; Que L^*

来源：Biochemical and Biophysical Research Communications, 2005, 338(1): 230-239.

DOI：10.1016/j.bbrc.2005.08.191

• non-heme iron
• oxygen activation
• post-translational modification
• self-hydroxylation
• ribonucleotide reductase
• alpha-ketoglutarate dependent enzymes

Recent years have seen considerable evolution in our understanding of the mechanisms of oxygen activation by non-heme iron enzymes, with high-valent iron-oxo intermediates coming to the forefront as formidably potent oxidants. In the absence of substrate, the generation of vividly colored chromophores deriving from the self-hydroxylation of a nearby aromatic amino acid for a number of these enzymes has afforded an opportunity to discern the conditions under which O(2) activation occurs to generate a high-valent iron intermediate, and has provided a basis for a rigorous mechanistic examination of the oxygenation process. Here, we summarize the current evidence for self-hydroxylation processes in both mononuclear non-heme iron enzymes and in mutant forms of ribonucleotide reductase, and place it within the context of our developing understanding of the oxidative transformations accomplished by non-heme iron centers.

• 出版日期2005-12-9