Abstract
Cytochrome- c oxidase aa 3 (CcO) from Paracoccus denitrificans interacts with tertiary butyl hydroperoxide (t-Bu–O–O–H, TBHP) by forming an adduct as indicated by an absorption shift at 408/432 nm and the induction of photochemical auto-reduction. The adduct was stable at room temperature for several days even under aerobic conditions. Upon irradiation (413 nm) of the adduct, a photoproduct, similar to the oxygenated mixed valence species (607 nm form), was formed, as indicated by the 418/442 and 607 nm signals in the absorption-difference spectrum. It is concluded that the adduct formation changes the photochemical properties of heme a 3. A molecular model for the binding mechanism of TBHP to CcO and for the photochemistry of heme a 3–TBHP adduct is proposed.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Bioenergetics
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