Post-translational self-hydroxylation: a probe for oxygen activation mechanisms in non-heme iron enzymes |
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Authors: | Farquhar Erik R Koehntop Kevin D Emerson Joseph P Que Lawrence |
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Affiliation: | Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, MN 55455, USA. |
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Abstract: | 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 O2 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. |
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Keywords: | Non-heme iron Oxygen activation Post-translational modification Self-hydroxylation Ribonucleotide reductase α-Ketoglutarate dependent enzymes |
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