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Article

Structural alterations of the heme environment of cytochrome P450cam and the Y96F mutant as deduced by resonance Raman spectroscopy.

Archives of biochemistry and biophysics - 1 Jan 2003

Niaura Gediminas, Reipa Vytas, Mayhew Martin P, Holden Marcia, Vilker Vincent L

Abstract excerpt

Resonance Raman spectroscopy at 2.5cm(-1) resolution was used to probe differences in wild-type and Y96F mutant P450cam (CYP101), both with and without bound camphor or styrene substrates. In the substrate-free state, the spin state equilibrium is shifted from 6-coordinate low spin (6CLS) toward more 5-coordinate high spin (5CHS) when tyrosine-96 in the substrate pocket is replaced by phenylalanine. About 25% of...

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PMID: 12464249
DOI: 10.1016/s0003-9861(02)00581-7

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