Manganese substituted Compound I of cytochrome P450 biomimetics: A comparative reactivity study of MnV-oxo versus MnIV-oxo species

2011 ◽  
Vol 507 (1) ◽  
pp. 4-13 ◽  
Author(s):  
Reza Latifi ◽  
Laleh Tahsini ◽  
Baharan Karamzadeh ◽  
Nasser Safari ◽  
Wonwoo Nam ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Compound I ◽  
Reactivity Study ◽  
Comparative Reactivity

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

A comparative reactivity study of microperoxidases based on hemin, mesohemin and deuterohemin

2005 ◽  
Vol 99 (3) ◽  
pp. 852-863 ◽  
Author(s):  
Ekaterina S. Ryabova ◽  
Patrik Rydberg ◽  
Matthias Kolberg ◽  
Espen Harbitz ◽  
Anne-Laure Barra ◽  
...  
Keyword(s):  
Reactivity Study ◽  
Comparative Reactivity

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.

scholarly journals Spectra and Kinetic Studies of the Compound I Derivative of Cytochrome P450 119

2008 ◽  
Vol 130 (40) ◽  
pp. 13310-13320 ◽  
Author(s):  
Xin Sheng ◽  
John H. Horner ◽  
Martin Newcomb
Keyword(s):  
Cytochrome P450 ◽  
Kinetic Studies ◽  
Compound I
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