Direct Resonance Raman Evidence for a Trans Influence on the Ferryl Fragment in Models of Compound I Intermediates of Heme Enzymes

1996 ◽  
Vol 118 (12) ◽  
pp. 2929-2935 ◽  
Author(s):  
Kazimierz Czarnecki ◽  
Shay Nimri ◽  
Zeev Gross ◽  
Leonard M. Proniewicz ◽  
James R. Kincaid
Keyword(s):  
Resonance Raman ◽  
Heme Enzymes ◽  
Compound I ◽  
Trans Influence ◽  
Direct Resonance

Resonance Raman Spectra of Legitimate Models for the Ubiquitous Compound I Intermediates of Oxidative Heme Enzymes

1999 ◽  
Vol 121 (34) ◽  
pp. 7953-7954 ◽  
Author(s):  
Kazimierz Czarnecki ◽  
James R. Kincaid ◽  
Hiroshi Fujii
Keyword(s):  
Raman Spectra ◽  
Resonance Raman ◽  
Heme Enzymes ◽  
Compound I ◽  
Resonance Raman Spectra

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.

Resonance Raman scattering from horseradish peroxidase compound I

1985 ◽  
Vol 107 (22) ◽  
pp. 6406-6407 ◽  
Author(s):  
W. Anthony Oertling ◽  
Gerald T. Babcock
Keyword(s):  
Horseradish Peroxidase ◽  
Raman Scattering ◽  
Resonance Raman ◽  
Resonance Raman Scattering ◽  
Compound I

A cryo-generated ferrous–superoxo porphyrin: EPR, resonance Raman and DFT studies

2015 ◽  
Vol 51 (62) ◽  
pp. 12407-12410 ◽  
Author(s):  
Takehiro Ohta ◽  
Jin-Gang Liu ◽  
Perumandla Nagaraju ◽  
Takashi Ogura ◽  
Yoshinori Naruta
Keyword(s):  
Raman Spectroscopy ◽  
Dft Calculations ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Dft Studies ◽  
Heme Enzymes

Cryo-generated ferrous–superoxy heme was studied by EPR, resonance Raman spectroscopy and DFT calculations, providing new insights into the structure–reactivity correlation of O2 activating heme enzymes and catalysts.

The resonance Raman spectrum of horseradish peroxidase compound I

1988 ◽  
Vol 110 (23) ◽  
pp. 7913-7915 ◽  
Author(s):  
Ki Jung. Paeng ◽  
James R. Kincaid
Keyword(s):  
Raman Spectrum ◽  
Horseradish Peroxidase ◽  
Resonance Raman ◽  
Resonance Raman Spectrum ◽  
Compound I

ENDOR Study of Oxoiron(IV) Porphyrin π-Cation Radical Complexes as Models for Compound I of Heme Enzymes

2009 ◽  
Vol 38 (1) ◽  
pp. 68-69 ◽  
Author(s):  
Akihiro Takahashi ◽  
Yasunori Ohba ◽  
Seigo Yamauchi ◽  
Hiroshi Fujii
Keyword(s):  
Cation Radical ◽  
Heme Enzymes ◽  
Compound I

Preparation and characterization of a novel oxoiron(IV) chlorin .pi.-cation radical complex. The first model for compound I of chlorin-containing heme enzymes

1992 ◽  
Vol 31 (20) ◽  
pp. 4042-4043 ◽  
Author(s):  
Shinji Ozawa ◽  
Yoshihito Watanabe ◽  
Isao Morishima
Keyword(s):  
Cation Radical ◽  
Heme Enzymes ◽  
Compound I ◽  
Radical Complex

scholarly journals Resonance Raman Spectroscopy of the Oxygenated Intermediates of Human CYP19A1 Implicates a Compound I Intermediate in the Final Lyase Step

2014 ◽  
Vol 136 (13) ◽  
pp. 4825-4828 ◽  
Author(s):  
Piotr J. Mak ◽  
Abhinav Luthra ◽  
Stephen G. Sligar ◽  
James R. Kincaid
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Compound I
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