Electronic Structure of Compound I in Human Isoforms of Cytochrome P450 from QM/MM Modeling

2005 ◽  
Vol 127 (37) ◽  
pp. 12900-12908 ◽  
Author(s):  
Christine M. Bathelt ◽  
Jolanta Zurek ◽  
Adrian J. Mulholland ◽  
Jeremy N. Harvey
Keyword(s):  
Electronic Structure ◽  
Cytochrome P450 ◽  
Compound I ◽  
Human Isoforms

New Features in the Catalytic Cycle of Cytochrome P450 during the Formation of Compound I from Compound 0

2005 ◽  
Vol 109 (42) ◽  
pp. 19946-19951 ◽  
Author(s):  
Devesh Kumar ◽  
Hajime Hirao ◽  
Sam P. de Visser ◽  
Jingjing Zheng ◽  
Dongqi Wang ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Catalytic Cycle ◽  
Compound I

scholarly journals A DFT Study of the Heme Role in the N-Demethylation of Theophylline Mediated by Compound I of Cytochrome P450

2007 ◽  
Vol 48 (4) ◽  
pp. 730-734 ◽  
Author(s):  
Mohamed Ismael ◽  
Carlos A. Del Carpio ◽  
Abdul Rajjak Shaikh ◽  
Hideyuki Tsuboi ◽  
Michihisa Koyama ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Dft Study ◽  
Compound I

Molecular engineering of cytochrome P450 and myoglobin for selective oxygenations

2004 ◽  
Vol 08 (03) ◽  
pp. 279-289 ◽  
Author(s):  
Takafumi Ueno ◽  
Takahiro Ohki ◽  
Yoshihito Watanabe
Keyword(s):  
Cytochrome P450 ◽  
Protein Engineering ◽  
Rational Design ◽  
Oxygen Carrier ◽  
Molecular Engineering ◽  
Heme Enzymes ◽  
Compound I ◽  
Dynamic Nature ◽  
Enzyme Substrate ◽  
First Time

Aspects of protein engineering of cytochrome P450 (P450) and myoglobin ( Mb ) to construct selective oxygenation catalysts have been described. Heme enzymes are known as biocatalysts for various oxidations but the design of substrate specificity has still remained one of the significant challenges because of dynamic nature of enzyme-substrate interactions. In particular, P450s are the most interesting targets among the heme enzymes because they are able to catalyze many types of monooxygenations such as hydroxylation, epoxidation, and sulfoxidation with high selectivity. Thus, many researchers have made efforts to convert the selectivity for natural substrates into that for unnatural substrates by several protein engineering approaches. On the other hand, we have reported a rational design of Mb to convert its oxygen carrier function into that of peroxidase or peroxygenase. The Mb mutants prepared in our work afford oxo-ferryl porphyrin radical cation (compound I) as observable species in Mb for the first time. Furthermore, some of the mutants we have constructed are useful for enantioselective oxygenations by oxygen transfer from the Mb -compound I to substrates.

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