Substrate activation for O2 reactions by oxidized metal centers in biology.

Abstract:

:The uncatalyzed reactions of O(2) (S = 1) with organic substrates (S = 0) are thermodynamically favorable but kinetically slow because they are spin-forbidden and the one-electron reduction potential of O(2) is unfavorable. In nature, many of these important O(2) reactions are catalyzed by metalloenzymes. In the case of mononuclear non-heme iron enzymes, either Fe(II) or Fe(III) can play the catalytic role in these spin-forbidden reactions. Whereas the ferrous enzymes activate O(2) directly for reaction, the ferric enzymes activate the substrate for O(2) attack. The enzyme-substrate complex of the ferric intradiol dioxygenases exhibits a low-energy catecholate to Fe(III) charge transfer transition that provides a mechanism by which both the Fe center and the catecholic substrate are activated for the reaction with O(2). In this Perspective, we evaluate how the coupling between this experimentally observed charge transfer and the change in geometry and ligand field of the oxidized metal center along the reaction coordinate can overcome the spin-forbidden nature of the O(2) reaction.

authors

Pau MY,Lipscomb JD,Solomon EI

doi

10.1073/pnas.0704191104

subject

Has Abstract

pub_date

2007-11-20 00:00:00

pages

18355-62

issue

47

eissn

0027-8424

issn

1091-6490

pii

0704191104

journal_volume

104

pub_type

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