Zobrazeno 1 - 10
of 417
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98dbb83d7c7563d230416af297a82820
https://doi.org/10.1007/s00214-011-1062-1
https://doi.org/10.1007/s00214-011-1062-1
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 ...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91a46f07bb52aa67faf10c78c386e70c
https://doi.org/10.1021/jp9811326
https://doi.org/10.1021/jp9811326
Publikováno v:
ChemInform. 27
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d950b14b5fbf13bbd15919c026322954
https://doi.org/10.1002/chin.199619027
https://doi.org/10.1002/chin.199619027
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8219d750db23c6c7c3936f62b9916168
https://pubmed.ncbi.nlm.nih.gov/10605835
https://pubmed.ncbi.nlm.nih.gov/10605835
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ab72de1b1341af22b07c93b68e8793f1
https://pubmed.ncbi.nlm.nih.gov/10512537
https://pubmed.ncbi.nlm.nih.gov/10512537
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::254bd8b56de3432cbccd70d56a6905a2
https://pubmed.ncbi.nlm.nih.gov/9514261
https://pubmed.ncbi.nlm.nih.gov/9514261
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9004d3e5ca13c0e625345dc2aff21d92
https://pubmed.ncbi.nlm.nih.gov/7629167
https://pubmed.ncbi.nlm.nih.gov/7629167
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7b96919cbda21c99959ad0d3d12afeb4
https://pubmed.ncbi.nlm.nih.gov/8142383
https://pubmed.ncbi.nlm.nih.gov/8142383
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1cb4e1dcac24c844c521087e488e74c0
https://pubmed.ncbi.nlm.nih.gov/8397197
https://pubmed.ncbi.nlm.nih.gov/8397197
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0ddd4b5863a88e8f6a4942229d6c5b8b
https://pubmed.ncbi.nlm.nih.gov/8384877
https://pubmed.ncbi.nlm.nih.gov/8384877