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The binding of cytochrome c peroxidase and ferricytochrome c. A spectrophotometric determination of the equilibrium association constant as a function of ionic strength

Autor: L B Vitello, J E Erman

Publikováno v: Journal of Biological Chemistry. 255:6224-6227

Complex formation between cytochrome c peroxidase and ferricytochrome c perturbs the optical absorption spectrum in the Soret band by about 2%. This perturbation can be utilized as a measure of the complex formed in solution and permits the determina

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::76645d24dd0b6a6ab7c885cd4ae1cc2c
https://doi.org/10.1016/s0021-9258(18)43726-x

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The cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Steady state kinetic mechanism

Autor: D S Kang, J E Erman

Publikováno v: Journal of Biological Chemistry. 257:12775-12779

Initial velocities for the cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide have been measured as functions of both the ferrocytochrome c (0.27-104 microM) and hydrogen peroxide (0.25-200 microM) concentrations at

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4cddcb459ed65ee7e4e297a5af29dfa3
https://doi.org/10.1016/s0021-9258(18)33580-4

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Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. Steady-state kinetics

Autor: H C, Jordi, J E, Erman

Publikováno v: Biochemistry. 13:3741-3745

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::190854a592e3f0a3e2144ee3a300e176
https://doi.org/10.1021/bi00715a019

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Raman difference spectroscopy of heme-linked ionizations in cytochrome c peroxidase

Autor: J A Shelnutt, James D. Satterlee, J E Erman

Publikováno v: Journal of Biological Chemistry. 258:2168-2173

The pH dependence of the oxidation-state marker line of hemoproteins is investigated in cytochrome c peroxidase with Raman difference spectroscopy. The frequency is sensitive to ionization of a group on the protein that regulates catalytic activity o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fcad67a475e77df9165a1eb768815438
https://doi.org/10.1016/s0021-9258(18)32903-x

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Temperature and pH dependence of the proton magnetic hyperfine resonances of cytochrome c peroxidase-cyanide. Evidence for hindered vinyl group rotation as a mediator of the enzymes activity

Autor: J D Satterlee, J E Erman

Publikováno v: Journal of Biological Chemistry. 258:1050-1056

Proton nmr studies of the hyperfine resonances of cytochrome c peroxidase reveal that two pH-dependent processes can be monitored. One of these is the simple pH titration of a resonance which has been previously assigned to the alpha-vinyl proton at

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d6cd2b6a7e307f72b5148105dad61cca
https://doi.org/10.1016/s0021-9258(18)33157-0

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Reduction of cytochrome c peroxidase compounds I and II by ferrocytochrome c. A stopped-flow kinetic investigation

Autor: F E Summers, J E Erman

Publikováno v: Journal of Biological Chemistry. 263:14267-14275

The oxidation of yeast cytochrome c peroxidase by hydrogen peroxide produces a unique enzyme intermediate, cytochrome c peroxidase Compound I, in which the ferric heme iron has been oxidized to an oxyferryl state, Fe(IV), and an amino acid residue ha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b5a0912a25fa278dc9f86e7b3f153864
https://doi.org/10.1016/s0021-9258(18)68216-x

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Proton hyperfine resonance assignments in cyanide-ligated cytochrome c peroxidase using the nuclear Overhauser effect

Autor: J D Satterlee, J E Erman, J S DeRopp

Publikováno v: Journal of Biological Chemistry. 262:11578-11583

The development of the proton nuclear Overhauser effect (NOE) for hyperfine shifted resonances of cyanide-ligated cytochrome c peroxidase (Saccharomyces cerevisiae) has been studied. In the pre-steady state regime, the major effects are due to primar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9776bc2d62fcb896ae53ba27a2868fca
https://doi.org/10.1016/s0021-9258(18)60847-6

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Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase

Autor: J E Erman, J D Satterlee

Publikováno v: Journal of Biological Chemistry. 256:1091-1093

Oxidation of cytochrome c peroxidase with hydrogen peroxide to form the initial oxidized intermediate, cytochrome c peroxidase compound I, drastically alters the proton hyperfine nmr spectrum. In contrast to studies of horseradish peroxidase, where t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f2cbb14dfc03dcce95f8c05b49593ed7
https://doi.org/10.1016/s0021-9258(19)69928-x

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