Studies on the mechanism of site I energy conservation.
1. Of the several iron-sulfur centers detected in the site I segment of the respiratory chain, centers N-2 and N-1a alone exhibit apparent phosphate-potential dependent half-reduction potentials, indicating their possible involvement in energy conservation. 2. At high phosphate potential, the apparent half-reduction potential of center N-2 shifts positively by 125 +/- 20 mV, while center N-1a shifts negatively by approximately 60 mV. 3. The redox state of individual iron-sulfur centers in various metabolic states was analyzed. Center N-2 is highly reduced (greater than 90%) in "state 4" mitochondria, while center N-1a stays mostly oxidized. 4. In a submitochondrial system, ATP addition induced reduction of center N-2 if the Eh of the suspension was poised from the high potential side of site I using the succinate/fumarate couple. In contrast, center N-2 was oxidized upon energization, if the Eh of the system was poised from the low potential side using the NADH/NAD couple. 5. Based on these redox behaviors of center N-2, a tentative hypothesis of site I energy transduction was proposed.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D010856:Columbidae; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D004735:Energy Transfer; D007501:Iron; D008931:Mitochondria, Muscle / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D009206:Myocardium; D010084:Oxidation-Reduction; D011199:Potentiometry; D013455:Sulfur
D013455:Sulfur; D000255:Adenosine Triphosphate; D007501:Iron