Zobrazeno 1 - 10
of 15
pro vyhledávání: '"D. B. Goodin"'
Autor:
G. M. Jensen, D. B. Goodin
Publikováno v:
Theoretical Chemistry Accounts. 130:1185-1196
Cytochrome c peroxidase (CCP) contains a five-coordinate heme active site. The reduction potential for the ferric to ferrous couple in CCP is anomalously low and pH dependent (Eo = ~−180 mV vs. S.H.E. at pH 7). The contribution of the protein envir
Publikováno v:
The Journal of Physical Chemistry B. 102:8221-8228
Despite very similar protein structures, ascorbate peroxidase (APX) and yeast cytochrome c peroxidase (CCP) stabilize different radical species during enzyme turnover. Both enzymes contain similar ...
Publikováno v:
ChemInform. 27
Publikováno v:
Journal of inorganic biochemistry. 76(3-4)
Electronic absorption and magnetic circular dichroism (MCD) spectroscopic data at 4 degrees C are reported for exogenous ligand-free ferric forms of cytochrome c peroxidase (CCP) in comparison with two other histidine-ligated heme proteins, horseradi
Publikováno v:
Biospectroscopy. 5
The addition of exogenous ligands to the ferric and ferrous states of yeast cytochrome c peroxidase (CCP) is investigated with magnetic circular dichroism (MCD) at 4 degrees C to determine the effect the protein environment may exercise on spectral p
Publikováno v:
Protein science : a publication of the Protein Society. 7(1)
A large-scale movement between "closed" and "open" conformations of a protein loop was observed directly with protein crystallography by trapping individual conformers through binding of an exogenous ligand and characterization with solution kinetics
Publikováno v:
The Journal of biological chemistry. 270(31)
A gene coding for the F172Y mutant of horseradish peroxidase isozyme C (HRP) has been constructed and expressed in both Spodoptera frugiperda (SF-9) and Trichoplusia ni egg cell homogenate (HighFive) cells. Homology modeling with respect to three per
Publikováno v:
Biochemistry. 33(13)
In the oxidized "ES" state of cytochrome c peroxidase, Trp-191 is reversibly oxidized to a stable cation free radical by the hypervalent heme. To explore the potential for engineering a binding site for heterocyclic compounds at this site, the mutant
Enhanced oxidation of aniline derivatives by two mutants of cytochrome c peroxidase at tryptophan 51
Autor:
J A, Roe, D B, Goodin
Publikováno v:
The Journal of biological chemistry. 268(27)
Two hyperactive mutants of cytochrome c peroxidase (CCP), W51F and W51A, catalyze the enhanced oxidation of a number of substituted anilines. The reaction of CCP compound ES with mesidine is biphasic, while similar reactions using compound II give mo
Autor:
D B, Goodin, D E, McRee
Publikováno v:
Biochemistry. 32(13)
The buried charge of Asp-235 in cytochrome c peroxidase (CCP) forms an important hydrogen bond to the histidine ligand of the heme iron. The Asp-His-metal interaction, which is similar to the catalytic triad of serine proteases, is found at the activ