Magnetic circular dichroism studies of the active site structure of hemoprotein H-450: Comparison to cytochrome P-450 and sensitivity of pH effects
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. Isolation and properties of a new, soluble, hemoprotein (H-450) from pig liver
2. Isolation and partial characterization of a new soluble b-type cytochrome (b9) from rat liver.
3. Immunological characterization of cytochrome H-450 in rat tissues.
4. Hemoprotein H-450 Identified as a Form of Cytochrome P-450 Having an Endogenous Ligand at the 6th Coordination Position of the Heme
5. Cytochrome P-450 and chloroperoxidase: thiolate-ligated heme enzymes. Spectroscopic determination of their active-site structures and mechanistic implications of thiolate ligation
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