P-450 binding to substrates camphor and linalool versus pressure.
The spin equilibrium of two bacterial cytochrome P-450 enzymes are compared by their visible spectra versus temperature and pressure. P-450 from Pseudomonas linalool shows a much weaker dependence on pressure than P-450 from P. putida which has camphor as substrate. The linalool system denatures at a higher pressure (3 kbar) than the camphor system (1 kbar) and shows a weaker dependence on external solvent conditions. The camphor system shows evidence of the binding of a second substrate molecule which reverses the effect of the first on the spin equilibrium. A model involving two substrate molecules is an alternative explanation of the apparent saturation with camphor of the spin equilibrium.[1]References
- P-450 binding to substrates camphor and linalool versus pressure. Marden, M.C., Hoa, G.H. Arch. Biochem. Biophys. (1987) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
