Syntheses and Catalytic Activities of New Cytochrome P-450 Model Compounds. Effect of Peptide Chains

1994 ◽  
Vol 67 (3) ◽  
pp. 742-747 ◽  
Author(s):  
Yasukazu Ohkatsu ◽  
Taiki Watanabe ◽  
Taiji Goto ◽  
Mitsuaki Wakita
Keyword(s):  
Model Compounds ◽  
Catalytic Activities ◽  
Cytochrome P 450

Epoxidation of olefins by cytochrome P-450 model compounds: kinetics and stereochemistry of oxygen atom transfer and origin of shape selectivity

1985 ◽  
Vol 107 (7) ◽  
pp. 2000-2005 ◽  
Author(s):  
James P. Collman ◽  
John I. Brauman ◽  
Bernard Meunier ◽  
Teruyuki Hayashi ◽  
Thomas Kodadek ◽  
...  
Keyword(s):  
Oxygen Atom ◽  
Shape Selectivity ◽  
Atom Transfer ◽  
Oxygen Atom Transfer ◽  
Model Compounds ◽  
Cytochrome P 450 ◽  
Epoxidation Of Olefins

Catalytic activities of metal oxides containing iron for hydrocracking coal model compounds and Taiheiyo coal

Fuel ◽  
1997 ◽  
Vol 76 (10) ◽  
pp. 913-918 ◽  
Author(s):  
Hiromi Matsuhashi ◽  
Hideo Nakamura ◽  
Kazushi Arata ◽  
Ryoichi Yoshida ◽  
Yosuke Maekawa
Keyword(s):  
Metal Oxides ◽  
Model Compounds ◽  
Catalytic Activities

scholarly journals Isolation of four forms of acetone-induced cytochrome P-450 in chicken liver by h.p.l.c. and their enzymic characterization

1990 ◽  
Vol 269 (1) ◽  
pp. 85-91 ◽  
Author(s):  
J F Sinclair ◽  
S Wood ◽  
L Lambrecht ◽  
N Gorman ◽  
L Mende-Mueller ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Chicken Liver ◽  
Terminal Amino Acid ◽  
Catalytic Activities ◽  
Terminal Amino ◽  
Cytochrome P 450 ◽  
Terminal Amino Acid Sequence

The purpose of this study was to purify and characterize the forms of cytochrome P-450 induced in chicken liver by acetone or ethanol. Using high performance liquid ion-exchange chromatography, we were able to isolate at least four different forms of cytochrome P-450 which were induced by acetone in chicken liver. All four forms of cytochrome P-450 proved to be distinct proteins, as indicated by their N-terminal amino acid sequences and their reconstituted catalytic activities. Two of these forms, also induced by glutethimide in chicken embryo liver, appeared to be cytochromes P450IIH1 and P450IIH2. Both of these cytochromes P-450 have identical catalytic activities towards benzphetamine demethylation. However, they differ in their abilities to hydroxylate p-nitrophenol and to convert acetaminophen into a metabolite that forms a covalent adduct with glutathione at the 3-position. Another form of cytochrome P-450 induced by acetone is highly active in the hydroxylation of p-nitrophenol and in the conversion of acetaminophen to a reactive metabolite, similar to reactions catalysed by mammalian cytochrome P450IIE. Yet the N-terminal amino acid sequence of this form has only 30-33% similarity with cytochrome P450IIE purified from rat, rabbit and human livers. A fourth form of cytochrome P-450 was identified whose N-terminal amino acid sequence and enzymic activities do not correspond to any mammalian cytochromes P-450 reported to be induced by acetone or ethanol.

Catalytic Activities of Calcined Iron Sulfates for Hydrocracking of Model Compounds of Coal

2001 ◽  
Vol 15 (6) ◽  
pp. 1523-1527 ◽  
Author(s):  
Hiromi Matsuhashi ◽  
Keiko Asari ◽  
Kazushi Arata
Keyword(s):  
Model Compounds ◽  
Catalytic Activities

Catalytic activities of human liver cytochrome P-450 IIIA4 expressed in Saccharomyces cerevisiae

Biochemistry ◽  
1990 ◽  
Vol 29 (51) ◽  
pp. 11280-11292 ◽  
Author(s):  
William R. Brian ◽  
Marie Agnes Sari ◽  
Masahiko Iwasaki ◽  
Tsutomu Shimada ◽  
Laurence S. Kaminsky ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Human Liver ◽  
Catalytic Activities ◽  
Liver Cytochrome ◽  
Cytochrome P 450
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