Purification and Characterization of Cytochrome P450 from an Isobutene-forming Microorganism, Rhodotorula minuta

Abstract

A cytochrome P450 was purified from microsomes of Rhodotorula minuta. The optical spectrum of the purified cytochrome was characteristic of a low-spin ferric heme protein. lsovalerate caused a type I spectral change in it. The amino-terminal sequence of the cytochrome was different from those of other known microsomal cytochrome P450s. These results indicate that the cytochrome, which is tentatively named P450rm, is a novel species of cytochrome P450.