Article
EPR spectrometry of cytochrome P450 2B4: effects of mutations and substrate binding.
Biochemical and biophysical research communications - 24 Sept 2000
LeLean J E, Moon N, Dunham W R, Coon M J
Abstract excerpt
The EPR spectra of NH(2)-terminal-truncated P450 cytochrome 2B4 and of several active site mutants that were previously shown to be profoundly altered in catalytic properties were determined. From these spectra it was seen that the truncated P450 2B4, like the full length cytochrome, exists as the low spin ferric form, but upon mutation of threonine 302 to alanine approximately 40% of the cytochrome is present as...
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