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

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.

authors

Farquhar ER,Koehntop KD,Emerson JP,Que L Jr

doi

10.1016/j.bbrc.2005.08.191

subject

Has Abstract

pub_date

2005-12-09 00:00:00

pages

230-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01917-0

journal_volume

338

pub_type

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