Abstract
Cytochrome P-450scc (CYP11A1) is known to exist in various conformational states. To study the accessibility of tyrosine residues to the solvent, second and fourth derivatives of cytochrome absorption spectra in the ultraviolet region were used. The measurements were carried out in the temperature range -10 to 40 °C and at two pH values (6.8 and 7.4). Our results indicate that the tyrosine residues of this enzyme are less accessible at higher temperatures as well as at higher pH, that is at conditions where the conformational equilibrium shifts to low-spin Fe(III) form(s). In other words, a more compact structure is attributable to the low-spin Fe(III) form(s) of P-450scc.
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