Structure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzyme

Bell, Stephen G., Yang, Wen, Yorke, Jake A., Zhou, Weihong, Wang, Hui, Harmer, Jeffrey, Copley, Rachel, Zhang, Aili, Zhou, Ruimin, Bartlam, Mark, Rao, Zihe and Wong, Luet-Lok (2012) Structure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzyme. Acta Crystallographica Section D: Biological Crystallography, 68 3: 277-291. doi:10.1107/S090744491200145X

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ303284_OA.pdf Full text (open access) application/pdf 2.13MB 0

Author Bell, Stephen G.
Yang, Wen
Yorke, Jake A.
Zhou, Weihong
Wang, Hui
Harmer, Jeffrey
Copley, Rachel
Zhang, Aili
Zhou, Ruimin
Bartlam, Mark
Rao, Zihe
Wong, Luet-Lok
Title Structure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzyme
Formatted title
Structure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzyme
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
1399-0047
Publication date 2012-03
Sub-type Article (original research)
DOI 10.1107/S090744491200145X
Open Access Status File (Publisher version)
Volume 68
Issue 3
Start page 277
End page 291
Total pages 15
Place of publication Malden, United States
Publisher Wiley-Blackwell Publishing
Language eng
Formatted abstract
CYP108D1 from Novosphingobium aromaticivorans DSM12444 binds a range of aromatic hydrocarbons such as phenanthrene, biphenyl and phenylcyclohexane. Its structure, which is reported here at 2.2 Å resolution, is closely related to that of CYP108A1 (P450terp), an [alpha]-terpineol-oxidizing enzyme. The compositions and structures of the active sites of these two enzymes are very similar; the most significant changes are the replacement of Glu77 and Thr103 in CYP108A1 by Thr79 and Val105 in CYP108D1. Other residue differences lead to a larger and more hydrophobic access channel in CYP108D1. These structural features are likely to account for the weaker [alpha]-terpineol binding by CYP108D1 and, when combined with the presence of three hydrophobic phenylalanine residues in the active site, promote the binding of aromatic hydrocarbons. The haem-proximal surface of CYP108D1 shows a different charge distribution and topology to those of CYP101D1, CYP101A1 and CYP108A1, including a pronounced kink in the proximal loop of CYP108D1, which may result in poor complementarity with the [2Fe-2S] ferredoxins Arx, putidaredoxin and terpredoxin that are the respective redox partners of these three P450 enzymes. The unexpectedly low reduction potential of phenylcyclohexane-bound CYP108D1 (-401 mV) may also contribute to the low activity observed with these ferredoxins. CYP108D1 appears to function as an aromatic hydrocarbon hydroxylase that requires a different electron-transfer cofactor protein.
Keyword Electron-transfer system
X-ray crystallography
Cytochrome P450Cam
Crystal-structure
Active-site
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Centre for Advanced Imaging Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 5 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 6 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Thu, 20 Jun 2013, 14:01:12 EST by System User on behalf of Centre for Advanced Imaging