STUDIES ON THE ORIENTATIONS OF THE MITOCHONDRIAL REDOX CARRIERS - ORIENTATION OF THE CHROMOPHORES OF CYTOCHROME-B-C1 COMPLEX WITH RESPECT TO THE PLANE OF A CYTOCHROME-B-C1 COMPLEX LIPID MODEL MEMBRANE
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作者:
ERECINSKA, M
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UNIV PENN, SCH MED, DEPT BIOCHEM & BIOPHYS, PHILADELPHIA, PA 19104 USAUNIV PENN, SCH MED, DEPT BIOCHEM & BIOPHYS, PHILADELPHIA, PA 19104 USA
ERECINSKA, M
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WILSON, DF
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UNIV PENN, SCH MED, DEPT BIOCHEM & BIOPHYS, PHILADELPHIA, PA 19104 USAUNIV PENN, SCH MED, DEPT BIOCHEM & BIOPHYS, PHILADELPHIA, PA 19104 USA
WILSON, DF
[1
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[1] UNIV PENN, SCH MED, DEPT BIOCHEM & BIOPHYS, PHILADELPHIA, PA 19104 USA
Orientations of the active site chromophores of the pig heart muscle mitochondrial cytochrome b-c1 complex incorporated into liposomes have been investigated in hydrated oriented multilayers of proteoliposome membranes using optical and EPR spectroscopy. The hemes of cytochromes c1 and b were oriented with the normal to their heme planes lying approximately in the plane of the proteoliposome membrane. Rieske''s Fe S center was oriented with the z-axis of the g tensor parallel to the plane of the membranes. The cytochrome b-c1 complex has a structural asymmetry which causes it to orient with respect to the lipid bilayer.