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Title: Nature of the ferryl heme in compounds I and II.
Authors: Gumiero, Andrea
Metcalfe, CLClive L.
Pearson, Arwen R.
Raven, Emma Lloyd
Moody, Peter C.
First Published: 14-Jan-2011
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Journal of Biological Chemistry, 2011, 286 (2), pp. 1260-1268
Abstract: Heme enzymes are ubiquitous in biology and catalyze a vast array of biological redox processes. The formation of high valent ferryl intermediates of the heme iron (known as Compounds I and Compound II) is implicated for a number of catalytic heme enzymes, but these species are formed only transiently and thus have proved somewhat elusive. In consequence, there has been conflicting evidence as to the nature of these ferryl intermediates in a number of different heme enzymes, in particular the precise nature of the bond between the heme iron and the bound oxygen atom. In this work, we present high resolution crystal structures of both Compound I and Compound II intermediates in two different heme peroxidase enzymes, cytochrome c peroxidase and ascorbate peroxidase, allowing direct and accurate comparison of the bonding interactions in the different intermediates. A consistent picture emerges across all structures, showing lengthening of the ferryl oxygen bond (and presumed protonation) on reduction of Compound I to Compound II. These data clarify long standing inconsistencies on the nature of the ferryl heme species in these intermediates.
DOI Link: 10.1074/jbc.M110.183483
eISSN: 1083-351X
Version: Publisher Version
Type: Journal Article
Rights: Copyright © 2011, American Society for Biochemistry and Molecular Biology. Deposited with reference to the publisher’s open access archiving policy.
Appears in Collections:Published Articles, Dept. of Biochemistry

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