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A mechanism for oxygen exchange between ligated oxometalloporphinates and bulk water.

Abstract：

:Oxygen exchange between high-valent metal-oxo complexes and bulk water has been monitored for nonligated model porphyrins (hemin, FeTDCPPS, MnTMPyP) and the axially ligated microperoxidase-8 (MP-8). Exchange extents up to 90% were measured for MP-8 in spite of the presence of an axial histidine ligand and accompanied by the formation of nonlabelled H(2)O(2) from H(2)(18)O(2). These results point to the existence of a mechanism for oxygen exchange between the high-valent iron-oxo complex and the solvent different from the so-called "oxo-hydroxo tautomerism." Regeneration of the primary oxidant, H(2)O(2), and oxygen exchange by axially ligated porphyrins can be explained by a mechanism involving the reversibility of compound I formation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Primus JL,Teunis K,Mandon D,Veeger C,Rietjens IM

doi

10.1006/bbrc.2000.2809

subject

Has Abstract

pub_date

2000-06-07 00:00:00

pages

551-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92809-2

journal_volume

272

pub_type

杂志文章

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