Modulation of cytochrome oxidase activity by inorganic and organic phosphate. |
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| Authors: | F Malatesta G Antonini P Sarti M Brunori |
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| Affiliation: | Department of Experimental Medicine and Biochemical Sciences, University of Rome Tor Vergata, Italy. |
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| Abstract: | The activity of cytochrome oxidase reconstituted into phospholipid vesicles has been studied as a function of orthophosphate, ATP and inositol hexakisphosphate concentrations. The respiratory-control ratio was found to be quite sensitive to these compounds and was inversely related to the anion concentration. This effect is related to a phosphate-dependent decrease in the rate constant for ferrocytochrome c oxidation observed in the presence of ionophores. The data cannot be interpreted simply on the basis of ionic strength, which is known to limit cytochrome c binding to cytochrome oxidase, since cytochrome oxidase-containing vesicles responded differently to phosphate depending on the energization state of the phospholipid membrane. |
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