Cytochrome c Peroxidase Compound ES Is Identical with Horseradish Peroxidase Compound I in Iron-Ligand Distances

M. Chance, B. Chance, T. Poulos, L. Powers

Research output: Contribution to journalArticle

80 Scopus citations

Abstract

X-ray absorption studies of compound ES of cytochrome c peroxidase show a short iron-oxygen distance of 1.67 ± 0.04 Å, an iron-histidine distance of 1.91 ± 0.03 Å, and an iron-pyrrole nitrogen average distance of 2.02 ± 0.02 Å. This is identical within the error with the reported structure of horseradish peroxidase compound I [Chance, B., Powers, L., Ching, Y., Poulos, T., Yamazaki, I., & Paul, K. G. (1984) Arch. Biochem. Biophys. 235, 596-611]. Comparisons of the structures of myoglobin peroxide [Chance, M., Powers, L., Kumar, C., & Chance, B. (1986) Biochemistry (preceding paper in this issue)], compound ES, and the intermediates of horseradish peroxidase reveal the possible mechanisms for the stabilization of the free radical species generated during catalysis. The proximal histidine regulates the structure and function of the pyrrole nitrogens and the heme, allowing for the formation and maintenance of the characteristic intermediates.

Original languageEnglish (US)
Pages (from-to)1266-1270
Number of pages5
JournalBiochemistry
Volume25
Issue number6
DOIs
StatePublished - Jan 1 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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