Tyrosine-96 as a natural spectroscopic probe of the cytochrome P-450cam active site.

doi:10.1021/bi00457a024

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Article

Tyrosine-96 as a natural spectroscopic probe of the cytochrome P-450cam active site.

Biochemistry - 6 Feb 1990

Atkins W M, Sligar S G

Abstract excerpt

The previously described correlation between the ferric spin equilibrium of cytochrome P-450cam and the environmental polarity of tyrosine residues (Fisher et al., 1986) has been further examined with the use of site-directed mutagenesis and active-site affinity reagents. Whereas the wild-type de...

Topics

Binding Sites
Camphor
Cytochrome P-450 Enzyme System
Escherichia coli
Mutation
Spectrophotometry, Ultraviolet
Substrate Specificity
Tyrosine

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