Journal ArticleDOI
Spectrum of chloroperoxidase compound I.
TLDR
The first visible spectrum of chloroperoxidase compound I is reported which has a peak at 689 nm as its most prominent feature.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1980-06-30. It has received 126 citations till now.read more
Citations
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Journal ArticleDOI
Heme-Containing Oxygenases
Journal ArticleDOI
Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins
Xiongyi Huang,John T. Groves +1 more
TL;DR: This review surveys the range of O2 activation processes mediated by heme proteins and model compounds with a focus on recent progress in the characterization and reactivity of important iron–oxygen intermediates.
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Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry.
TL;DR: It is suggested that the CPO-II protonated ferryl is a good model for the rebound intermediate in the P450 oxygenation cycle; with elevated pKa values after one-electron reduction, thiolate-ligation ferryl radicals are competent to oxygenate saturated hydrocarbons at potentials that can be tolerated by folded polypeptide hosts.
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Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle.
TL;DR: Spectroscopically characterize the oxidized states of MnP compounds I, II, and III and clarify the role of Mn in the catalytic cycle of the enzyme, indicating that Mn(II) serves as an obligatory substrate for MnP compound II, allowing the enzyme to complete its catalysttic cycle.
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The Elusive Oxidant Species of Cytochrome P450 Enzymes: Characterization by Combined Quantum Mechanical/Molecular Mechanical (QM/MM) Calculations
Jan Schöneboom,Hai Lin,Nathalie Reuter,Walter Thiel,Shimrit Cohen,François Ogliaro,Sason Shaik +6 more
TL;DR: Combined quantum mechanical/molecular mechanical (QM/MM) calculations of Compound I of cytochrome P450(cam) in the full enzyme environment as well as density functional studies of the isolated QM region show that the protein environment and its specific hydrogen bonding to the cysteinate ligand are crucial for sustaining the Fe-S bond and for preventing the full oxidation of the sulfur.
References
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Journal ArticleDOI
Chloroperoxidase I. ISOLATION AND PROPERTIES OF THE CRYSTALLINE GLYCOPROTEIN
David R. Morris,Lowell P. Hager +1 more
TL;DR: Chloroperoxidase from Caldariomyces fumago has been isolated in crystalline form and Chromatography of acid hydrolysates reveals that glucosamine and arabinose are major constituents.
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Chloroperoxidase. II. Utilization of halogen anions.
TL;DR: Results indicate that fluoride ion can compete for both the hydrogen peroxide- and the halogen anion-binding sites on chloroperoxidase.
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Chloroperoxidase. VII. Classical peroxidatic, catalatic, and halogenating forms of the enzyme.
TL;DR: Results indicate that Compound I of chloroperoxidase may contain a reactive oxygen atom, and by analogy with organic mechanisms for the decomposition of peracids, these results indicate that the enzyme also oxidizes ethanol to form acetaldehyde.
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Chloroperoxidase VIII. FORMATION OF PEROXIDE AND HALIDE COMPLEXES AND THEIR RELATION TO THE MECHANISM OF THE HALOGENATION REACTION
TL;DR: The spectral changes caused by the addition of hydrogen peroxide and halide salts to chloroperoxidase have been investigated and discussed in relation to the halogenation activity of the enzyme.
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The P-450 Nature of the Carbon Monoxide Complex of Ferrous Chloroperoxidase
TL;DR: The spectral similarities described here indicate that both proteins provide quite similar environments for the heme prosthetic group and compare favorably with respect to physical properties such as molecular weight, high content of acidic amino acids, and low isoelectric point.