Comparison of heme environment at the putative distal region of P-450s utilizing their external and internal nitrogenous ligand bound forms.

doi:10.1016/0167-4838(94)90050-7

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Article

Comparison of heme environment at the putative distal region of P-450s utilizing their external and internal nitrogenous ligand bound forms.

Biochimica et biophysica acta - 20 Jul 1994

Imai Y, Fukuda T, Komori M, Nakamura M

Abstract excerpt

Thr-303 to Lys-mutated P-450 2E1, as well as Thr-301 to Lys-mutated P-450 2C2, had absorption spectra characteristic of a nitrogenous ligand-bound form of P-450, such as the pyridine complex of P-450 2E1; (i) in the ferric state, the red-shifted Soret band, compared with the typical low-spin type...

Topics

Base Sequence
Cytochrome P-450 CYP2E1
Cytochrome P-450 Enzyme System
Heme
Ligands
Molecular Sequence Data
Mutation
Nitriles
Oxidoreductases, N-Demethylating
Spectrophotometry

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