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Type: Journal article
Title: Purification, crystallization and preliminary X-ray analysis of cytochrome P450 219A1 from Novosphingobium aromaticivorans DSM 12444
Author: Hong, C.
Bell, S.
Yang, W.
Wang, H.
Hao, Y.
Li, X.
Zhou, W.
Bartlam, M.
Wong, L.
Citation: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 2009; 65(4):364-367
Publisher: Blackwell Munksgaard
Issue Date: 2009
ISSN: 1744-3091
Statement of
Chuan Hong, Stephen G. Bell, Wen Yang, Hui Wang, Yiming Hao, Xin Li, Weihong Zhou, Mark Bartlam, and Luet-Lok Wong
Abstract: 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 (C15H22O), a sesquiterpenoid ketone derivative, is a potential substrate for CYP219A1, inducing a [greater-than or equal to]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 P6, 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.
Keywords: cytochrome P450 219A1; Novosphingobium aromaticivorans DSM 12444
Rights: © 2009 International Union of Crystallography
RMID: 0020121284
DOI: 10.1107/S1744309109005648
Appears in Collections:Chemistry and Physics publications

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