Abstract
Membraneous cytochrome oxidase (E.C. 1.9.3.1) was labelled with iodoacetamide and maleimide spin labels and solubilized with Triton X-100. On reduction, the EPR spectrum of the original membraneous oxidase was shifted toward the less strongly immobilized form as measured with either label.
After solubilization, the EPR spectrum in the oxidized state was unchanged. The change of conformation upon reduction was either eliminated (if measured with iodoacetamide label) or was reversed, i.e., changed toward the strongly immobilized spectrum, if measured with maleimide label.
This finding indicates that solubilization does not alter the conformation of the oxidized form of cytochrome oxidase, but does change the preferred conformation of the reduced form.
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Kirkpatrick, F.H., Jacobs, E.E. Effect of reduction and solubilization on the conformation of cytochrome oxidase. J Bioenerg Biomembr 1, 413–422 (1970). https://doi.org/10.1007/BF01516904
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DOI: https://doi.org/10.1007/BF01516904