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  • Title: Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase.
    Author: Ullah AJ, Murray RI, Bhattacharyya PK, Wagner GC, Gunsalus IC.
    Journal: J Biol Chem; 1990 Jan 25; 265(3):1345-51. PubMed ID: 2295633.
    Abstract:
    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.
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