ISSN:
1573-6881
Keywords:
cytochrome
;
oxidase
;
mitochondria
;
structure membrane
;
protein
;
subunits
;
oxidation-reduction
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract We report here studies which characterize further the interaction ofN,N′-dicyclohexylcarbodiimide with cytochromec oxidase leading to inhibition of H+ translocation by the enzyme. Further evidence is presented to show that the inhibition results from a real interaction of DCCD with the enzyme and cannot be accounted for by uncoupling and, contrary to recent criticisms, this interaction occurs specifically with subunit III of the enzyme even at relatively high inhibitor-to-enzyme stoichiometries. Use of a spin-label analogue of DCCD has enabled us to demonstrate that the carbodiimide-binding site is highly apolar and may not lie on the pathway of electron transfer.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00743201
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