Active site model of cytochrome P-450 LM2
- 9 February 1988
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 150 (3) , 996-1005
- https://doi.org/10.1016/0006-291x(88)90727-9
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Cytochrome P-450 Related to P-4504 from Phenobarbital-Treated Rabbit Liver: Molecular Cloning of cDNA and Characterization of Cytochrome P-450 Obtained by Its Expression in Yeast Cells1The Journal of Biochemistry, 1987
- The P450 Gene Superfamily: Recommended NomenclatureDNA, 1987
- The interaction between phenylalanine rings in proteinsFEBS Letters, 1985
- Optimized monopole expansions for the representation of the electrostatic properties of polypeptides and proteinsJournal of Computational Chemistry, 1985
- Aromatic-Aromatic Interaction: A Mechanism of Protein Structure StabilizationScience, 1985
- Relation between the structure of benzphetamine analogues and their binding properties to cytochrome P-450 LM2Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Spin state control of cytochrome P-450 reduction and catalytic activity in a reconstituted P-450 LM2 system as induced by a series of benzphetamine analoguesChemico-Biological Interactions, 1985
- Isolation and sequence analysis of three cloned cDNAs for rabbit liver proteins that are related to rabbit cytochrome P-450 (form 2), the major phenobarbital-inducible formBiochemistry, 1984
- Identification of the ligand trans to thiolate in cytochrome P‐450 LM2 by chemical modificationFEBS Letters, 1983
- THE STRUCTURE OF WATER AND HYDROPHOBIC BONDING IN PROTEINS. III. THE THERMODYNAMIC PROPERTIES OF HYDROPHOBIC BONDS IN PROTEINS1,2The Journal of Physical Chemistry, 1962