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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. 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. J. Biol. Chem. (1990) [Pubmed]
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