Abstract
The cytochrome c oxidase binding site on cytochrome c. Differential chemical modification of lysine residues in free and oxidase-bound cytochrome c.
Highlights
IntroductionFerricytochrome c forms complexes with isolated cytochrome c oxidase (ferrocytochrome czoxygen oxidoreductase, EC 1.9.3.1) with stoichiometries of 1:l and
Ferricytochrome c forms complexes with isolated cytochrome c oxidase with stoichiometries of 1:l and
A sample of cytochrome c oxidase saturated with cytochrome c was chromatographed on a column of Sephadex G-75 which had been equilibrated with triethanolamine buffer devoid of cytochrome c
Summary
Ferricytochrome c forms complexes with isolated cytochrome c oxidase (ferrocytochrome czoxygen oxidoreductase, EC 1.9.3.1) with stoichiometries of 1:l and. These complexes have been studied in order to localize the binding site for cytochrome c oxidase on the cytochrome c molecule. The shielding effect of the oxidase was greatest toward residue 13 Based on this information we propose a binding site for cytochrome c oxidase which spans over the top and part of the left-hand side of the cytochrome c molecule. 252, 4619-4636.) The binding site involves part of the NHz-terminal helix at the top right of the heme crevice, lysine residue 13 above the exposed heme edge, the section around residues 86 to 88 at the top left of the heme crevice and part of the left-hand surface of the molecule. A mechanism of electron transfer from heme c via the exposed heme edge (pyrrole ring II) to cytochrome c oxidase would be compatible with the present findings
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