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Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction
Journal of Biomolecular NMR, 2013Here we present a solution NMR study of the complex between yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP), a paradigm for understanding the biological electron transfer. Performed for the first time, the CcP-observed heteronuclear NMR experiments were used to probe the Cc binding in solution.
A. Volkov, N. Nuland
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Biochemistry, 2019
Mitochondrial cytochrome c is a highly conserved protein in eukaryotes. Certain functions of cytochrome c have been tuned during evolution. For instance, the intrinsic peroxidase activity of human cytochrome c is much lower than that of the yeast ...
Haotian Lei +3 more
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Mitochondrial cytochrome c is a highly conserved protein in eukaryotes. Certain functions of cytochrome c have been tuned during evolution. For instance, the intrinsic peroxidase activity of human cytochrome c is much lower than that of the yeast ...
Haotian Lei +3 more
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Journal of Physical Chemistry B, 2019
The immobilization of proteins on inorganic supports is attracting increasing interest since the realization of active surfaces finds application in enzyme-assisted catalysis, environmental sciences, and medical fields. In the present study, cytochrome c
L. Tarpani +5 more
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The immobilization of proteins on inorganic supports is attracting increasing interest since the realization of active surfaces finds application in enzyme-assisted catalysis, environmental sciences, and medical fields. In the present study, cytochrome c
L. Tarpani +5 more
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Methionine modification in cytochrome-c peroxidase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988Hydrogen peroxide oxidizes Met-119, Met-230 and Met-231 to the sulfoxide derivatives with equal initial rates in apocytochrome-c peroxidase at pH 4 in 0.1 M sodium acetate buffer. No detectable oxidation of Met-163 and Met-172 occurs under these conditions.
K, Kim, J E, Erman
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Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association
Science, 1988Brownian dynamics computer simulations of the diffusional association of electron transport proteins cytochrome c (cyt c) and cytochrome c peroxidase (cyt c per) were performed. A highly detailed and realistic model of the protein structures and their electrostatic interactions was used that was based on an atomic-level spatial description.
S H, Northrup, J O, Boles, J C, Reynolds
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The oxidation of cytochrome c by cytochrome c peroxidase
Archives of Biochemistry and Biophysics, 1960Abstract 1. 1. The reaction between cytochrome c and cytochrome c peroxidase is first order in cytochrome c. 2. 2. The reaction is inhibited by both oxidized and reduced cytochrome c. 3. 3. The dependence of the reaction rate on ionic strength suggests that the reaction occurs at oppositely charged active sites on the two proteins. 4.
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Physical Chemistry, Chemical Physics - PCCP, 2015
Choline dioctylsulfosuccinate [Cho][AOT] (a surface active ionic liquid) has been found to induce all-α to α + β conformational transition in the secondary structure of enzyme cytochrome c (Cyt c) with an enhanced peroxidase activity in its aqueous ...
Pankaj Bharmoria +4 more
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Choline dioctylsulfosuccinate [Cho][AOT] (a surface active ionic liquid) has been found to induce all-α to α + β conformational transition in the secondary structure of enzyme cytochrome c (Cyt c) with an enhanced peroxidase activity in its aqueous ...
Pankaj Bharmoria +4 more
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Peroxidase activity of mitochondrial cytochrome c oxidase
Biochemistry (Moscow), 2007Mitochondrial cytochrome c oxidase is able to oxidize various aromatic compounds like o-dianisidine, benzidine and its derivatives (diaminobenzidine, etc.), p-phenylenediamine, as well as amidopyrine, melatonin, and some other pharmacologically and physiologically active substances via the peroxidase, but not the oxidase mechanism.
T V, Vygodina, A A, Konstantinov
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Cytochrome c peroxidase from Methylococcus capsulatus Bath
Archives of Microbiology, 1997A bacterial cytochrome c peroxidase was purified from the obligate methanotroph Methylococcus capsulatus Bath in either the fully oxidized or the half reduced form depending on the purification procedure. The cytochrome was a homo-dimer with a subunit mol mass of 35.8 kDa and an isoelectric point of 4.5.
J A, Zahn +4 more
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Cytochrome c′-type cytochrome-c peroxidase derived from Nitrosomonas europaea
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986Abstract From Nitrosomonas europaea , a cytochrome c ′-type haem protein has been purified which has cytochrome- c peroxidase (ferrocytochrome- c :hydrogen-peroxide oxidoreductase, EC 1.11.1.5) activity. The protein has haem c and shows the high-spin-type absorption spectra: it shows absorption peaks at 400, 500 and 640 nm in the oxidized form ...
Takeshi Yamazaki +2 more
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