A mononuclear nonheme iron(iv)-oxo complex which is more reactive than cytochrome P450 model compound I

2011 ◽  
Vol 2 (6) ◽  
pp. 1039 ◽  
Author(s):  
Mi Sook Seo ◽  
Nam Hee Kim ◽  
Kyung-Bin Cho ◽  
Jeong Eun So ◽  
Seon Kyung Park ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Model Compound ◽  
Nonheme Iron ◽  
Compound I

scholarly journals A Systematic Account on Aromatic Hydroxylation by a Cytochrome P450 Model Compound I: A Low-Pressure Mass Spectrometry and Computational Study

2016 ◽  
Vol 22 (51) ◽  
pp. 18608-18619 ◽  
Author(s):  
Fabián G. Cantú Reinhard ◽  
Mala A. Sainna ◽  
Pranav Upadhyay ◽  
G. Alex Balan ◽  
Devesh Kumar ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cytochrome P450 ◽  
Model Compound ◽  
Computational Study ◽  
Low Pressure ◽  
Compound I ◽  
Systematic Account ◽  
Aromatic Hydroxylation

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.

scholarly journals Cytochrome P450 Alkane Hydroxylases of the CYP153 Family Are Common in Alkane-Degrading Eubacteria Lacking Integral Membrane Alkane Hydroxylases

2006 ◽  
Vol 72 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Jan B. van Beilen ◽  
Enrico G. Funhoff ◽  
Alexander van Loon ◽  
Andrea Just ◽  
Leo Kaysser ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Pseudomonas Putida ◽  
Chain Length ◽  
Nonheme Iron ◽  
Cytochrome P450 Enzymes ◽  
Medium Chain ◽  
Ferredoxin Reductase ◽  
Medium Chain Length ◽  
Reductase Gene ◽  
Alkane Hydroxylases

ABSTRACT Several strains that grow on medium-chain-length alkanes and catalyze interesting hydroxylation and epoxidation reactions do not possess integral membrane nonheme iron alkane hydroxylases. Using PCR, we show that most of these strains possess enzymes related to CYP153A1 and CYP153A6, cytochrome P450 enzymes that were characterized as alkane hydroxylases. A vector for the polycistronic coexpression of individual CYP153 genes with a ferredoxin gene and a ferredoxin reductase gene was constructed. Seven of the 11 CYP153 genes tested allowed Pseudomonas putida GPo12 recombinants to grow well on alkanes, providing evidence that the newly cloned P450s are indeed alkane hydroxylases.

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