Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface.
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TLDR
The results are rationalized by H2O2-dependent formation of a protein radical that combines with molecular oxygen to give a protein-peroxy radical that oxidizes styrene.About:
This article is published in Journal of Biological Chemistry.The article was published on 1985-08-05 and is currently open access. It has received 169 citations till now. The article focuses on the topics: Styrene oxide & Styrene.read more
Citations
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Peroxidase-modified electrodes: Fundamentals and application
TL;DR: In this paper, the peroxidase-modified amperometric electrodes have been widely studied and developed, not only because of hydrogen and organic peroxides are important analytes but also because of the key role of hydrogen peroxide detection in coupled enzyme systems, in which the peroxide is formed as the product of the enzymatic reaction.
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The toxicities of native and modified hemoglobins.
Johannes Everse,Nelson Hsia +1 more
TL;DR: The conditions under which reactive species of hemoglobin may be formed in vivo, their potential reactivity, and whether their individual or combined oxidative activities could account for the biological damage that is observed in vivo following hemoglobin transfusions are considered.
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Control of the catalytic activity of prosthetic heme by the structure of hemoproteins
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Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.
Shin-ichi Adachi,Shingo Nagano,Koichiro Ishimori,Yoshihito Watanabe,Isao Morishima,Tsuyoshi Egawa,Teizo Kitagawa,Ryu Makino +7 more
TL;DR: Histidine-93(F8) in human myoglobin (Mb), which is the proximal ligand of the heme iron, has been replaced with cysteine or tyrosine by site-directed mutagenesis and exhibit the altered axial ligation analogous to P-450, chloroperoxidase, and catalase.
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Free radicals in iron-containing systems.
TL;DR: An attacking role for superoxide dismutase is proposed in the phagocytic process in which it may serve as an intermediate enzyme between NADPH oxidase and myeloperoxidase.
References
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The Generation of Superoxide Radical during the Autoxidation of Hemoglobin
Hara P. Misra,Irwin Fridovich +1 more
TL;DR: Clostridial and spinach ferredoxins, reduced enzymatically by the action of ferredoxin-TPN+ oxidoreductase, have been shown to carry out the univalent reduction of oxygen.
Book
Hemoglobin : structure, function, evolution, and pathology
TL;DR: Come with us to read a new book that is coming recently, this is a new coming book that many people really want to read will you be one of them?
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Catalytic asymmetric epoxidations with chiral iron porphyrins
John T. Groves,Richard S. Myers +1 more
TL;DR: Epoxydation asymetrique d'olefines prochirales par des porphyrines de fer chirales and par des composes iodosyles.
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Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P-450.
TL;DR: Data obtained are in accord with a peroxidase-like mechanism for the action of cytochrome P-450, which catalyzes the hydroperoxide-dependent hydroxylation of a variety of substrates in the absence of NADPH, NADPHcytochromeP-450 reductase, and molecular oxygen.
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