Open AccessPurification, crystallization and preliminary X‐ray analysis of cytochrome P450 219A1 from Novosphingobium aromaticivorans DSM 12444
Author(s) -
Hong Chuan,
Bell Stephen G.,
Yang Wen,
Wang Hui,
Hao Yiming,
Li Xin,
Zhou Weihong,
Bartlam Mark,
Wong LuetLok
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109005648
Subject(s) - cytochrome p450 , crystallography , enzyme , stereochemistry , chemistry , biology , biochemistry
Cytochrome P450 enzymes catalyze a variety of reactions and are widely distributed in living organisms. In recent studies, the first members of five new families of cytochrome P450 enzymes have been identified, including cytochrome P450 219A1 (CYP219A1) from Novosphingobium aromaticivorans DSM 12444. It has also been reported that isolongifolen‐9‐one (C 15 H 22 O), a sesquiterpenoid ketone derivative, is a potential substrate for CYP219A1, inducing a ≥95% shift of the haem spin state to high spin upon binding. The CYP219A1 protein has been crystallized and single crystals have been studied by X‐ray crystallography. Diffraction data were collected to 2.4 Å resolution. The crystals belonged to space group P 6, with unit‐cell parameters a = 93.1, b = 93.1, c = 98.0 Å. Preliminary X‐ray diffraction data analysis revealed that the asymmetric unit contained one protein molecule.