X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes

Linda S Powers, L. Powers, C. Kumar, B. Chance

Research output: Contribution to journalArticle

86 Citations (Scopus)

Abstract

X-ray absorption studies of myoglobin peroxide show that although it is not identical with compound I or II of horseradish peroxidase [Chance, B., Powers, L., Ching, Y., Poulos, T., Yamazaki, I., & Paul, K. G. (1984) Arch. Biochem. Biophys. 235, 596-611], it has some structural features in common with both. As seen in compound I, the Fe-O distance is short, but the iron-pyrrole nitrogen distance is contracted with a longer iron-histidine distance like compound II. The iron has a higher oxidation state than Fe3+, suggesting an oxyferryl ion type species. Comparison of the structures of various peroxidase and myoglobin compounds points out systematic differences that may explain the catalytic activity of the π cation radical as well as some of the differences between globins and heme enzymes.

Original languageEnglish (US)
Pages (from-to)1259-1265
Number of pages7
JournalBiochemistry
Volume25
Issue number6
StatePublished - 1986
Externally publishedYes

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Globins
X ray absorption
Heme
Iron
X-Rays
Enzymes
Pyrroles
Myoglobin
Arches
Horseradish Peroxidase
Histidine
Peroxidase
Cations
Catalyst activity
Nitrogen
Ions
Oxidation
peroxymyoglobin

ASJC Scopus subject areas

  • Biochemistry

Cite this

X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes. / Powers, Linda S; Powers, L.; Kumar, C.; Chance, B.

In: Biochemistry, Vol. 25, No. 6, 1986, p. 1259-1265.

Research output: Contribution to journalArticle

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