Temperature effects on optical absorption and circular dichroism of cytochrome P-450scc from bovine adrenocortical mitochondria.
Temperature-dependent spin changes of the heme iron atom on cytochrome P-450scc were studied by optical absorption and circular dichroism measurements. The optical absorption and circular dichroism spectra of cholesterol-free cytochrome P-450scc did not change between 10 and 26 degrees C. In contrast, the absorbance at 390 nm and the ellipticity at 330 nm of cholesterol-bound cytochrome P-450scc decreased upon temperature elevation, and the absorbance at 424 nm correspondingly increased. These spectral changes were reversible in respect of temperature. The far-ultraviolet circular dichroism spectra of both cholesterol-bound and -free cytochrome P-450scc were not affected by temperature. In addition, bound cholesterol molecule is not released from the cytochrome molecule by increasing temperature. From these results, we propose that temperature modulates specific interactions between the heme protein and bound cholesterol rather than the gross secondary structural changes of the protein.
D000302:Adrenal Cortex / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D011487:Protein Conformation; D013053:Spectrophotometry; D013696:Temperature
D003577:Cytochrome P-450 Enzyme System