Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase

Ullah, A. J. ; Murray, R. I. ; Bhattacharyya, P. K. ; Wagner, G. C. ; Gunsalus, I. C. (1990) Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase Journal of Biological Chemistry, 265 (3). pp. 1345-1351. ISSN 0021-9258

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The cytochrome P-450 heme-thiolate monooxygenases that hydroxylate monoterpene hydrocarbon groups are effective models for the cytochrome P-450 family. We have purified and characterized the three proteins from a P-450-dependent linalool 8-methyl hydroxylase in Pseudomonas putida (incognita) strain PpG777. The proteins resemble the camphor 5-exohydroxylase components in chemical and physical properties; however, they show neither immunological cross-reactivity nor catalytic activity in heterogenous recombination. These two systems provide an excellent model to probe more deeply the heme-thiolate reaction center, molecular domains of substrate specificity, redox-pair interactions, and the regulation of the reaction cycle.

Item Type:Article
Source:Copyright of this article belongs to The American Society for Biochemistry and Molecular Biology.
ID Code:30864
Deposited On:27 Dec 2010 08:04
Last Modified:17 May 2016 13:28

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