Spectrophotometric Characterization of Intermediate Redox States of Cytochrome Oxidasea
- 17 December 1988
- journal article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 550 (1) , 150-160
- https://doi.org/10.1111/j.1749-6632.1988.tb35331.x
Abstract
The spectrophotometric characteristics of hemes a and a3 in cytochrome oxidase have been examined over the range 380 nm to 900 nm. Difference spectra (relative to the oxidized form) are presented for ferrous, high-spin oxidized, low-spin oxidized, early "pulsed," late "pulsed," and two-peroxide-treated states of the enzyme. Comparisons indicate that the decay product of the initial peroxide complex of the enzyme is identical to a low-spin pulsed form of the enzyme. A high-spin pulsed form of the enzyme persists for several hours to days after preparation.Keywords
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