Feb 16, 1976

Kinetic studies on cytochrome c oxidase by combined epr and reflectance spectroscopy after rapid freezing

Biochimica Et Biophysica Acta
H BeinertC R Hartzell

Abstract

1. Techniques and experiments are described concerned with the millisecond kinetics of EPT-detectable changes brought about in cytochrome c oxidase by reduced cytochrome c and, after reduction with various agents, by reoxidation with O2 or ferricyanide. Some experiments in the presence of ligands are also reported. Light absorption was monitored by low-temperature reflectance spectroscopy. 2. In the rapid phase of reduction of cytochrome c oxidase by cytochrome c (less than 50 ms) approx. 0.5 electron equivalent per heme a is transferred mainly to the low-spin heme component of cytochrome c oxidase and partly to the EPR-detectable copper. In a slow phase (less than 1 s) the copper is reoxidized and high-spin ferric heme signals appear with a predominant rhombic component. Simultaneously the absorption band at 655 nm decreases and the Soret band at 444 nm appears between the split Soret band (442 and 447 nm) of reduced cytochrome a. 3. On reoxidation of reduced enzyme by oxygen all EPR and optical features are restored within 6 ms. On reoxidation by O2 in the presence of an excess of reduced cytochrome c, states can be observed where the low-spin heme and copper signals are largely absent but the absorption at 655 nm is maximal,...Continue Reading

Mentioned in this Paper

CYCS
COX1
Cytochrome C Oxidase
Cytochrome c Oxidase Subunit VIa
Cytochrome a Activity
Activated T Cell Autonomous Cell Death
Isocyanides
Cytochrome a
Cytochrome c Group
Protein Conformation

About this Paper

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