Heat treatment of cytochrome c oxidase perturbs the Cu sub(A) site and affects proton pumping behavior
It has been previously reported that mild heat treatment (43 degree C for ca. 60 min) abolishes the proton pumping activity of cytochrome c oxidase while leaving the oxidase activity and cytochromes a and a sub(3) unperturbed. The authors herein describe the effects of this heat treatment on the ele...
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| Published in: | Biochemistry (Easton) Vol. 27; no. 19; pp. 7538 - 7546 |
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| Main Authors: | , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
01-01-1988
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| Online Access: | Get full text |
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| Summary: | It has been previously reported that mild heat treatment (43 degree C for ca. 60 min) abolishes the proton pumping activity of cytochrome c oxidase while leaving the oxidase activity and cytochromes a and a sub(3) unperturbed. The authors herein describe the effects of this heat treatment on the electron paramagnetic resonance (EPR) and optical absorption signatures of the redox-active metal centers in the enzyme. They find that heat treatment of the oxidized enzyme causes a local structural perturbation at the Cu sub(A) site. After heat treatment, the enzyme sample contains three subpopulations, each of which has a different structure at Cu sub(A). |
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| Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-1 |
| ISSN: | 0006-2960 |