Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Richard A. Tschirret-Guth"'
Autor:
Alexei V. Buevich, Richard A. Tschirret-Guth, Mark T. Cancilla, Josien Hubert B, Qing Chen, Koppara Samuel, Ann Thomas, Wei Tong, Harry R. Chobanian, Kaushik Mitra, Jackie Shang
Publikováno v:
Chemical research in toxicology. 33(1)
MK-8666, a selective GPR40 agonist developed for the treatment of type 2 diabetes mellitus, was discontinued in phase I clinical trials due to liver safety concerns. To address whether chemically reactive metabolites played a causative role in the ob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8e042e02e861ca7bcbc70f5f6208ca9
https://pubmed.ncbi.nlm.nih.gov/31566356
https://pubmed.ncbi.nlm.nih.gov/31566356
Autor:
Richard A. Tschirret-Guth, Michael R. Gunther, Olivier M. Lardinois, Paul R. Ortiz de Montellano
Publikováno v:
Chemical Research in Toxicology. 16:652-660
The 3,5-dibromo-4-nitrosobenzenesulfonate (DBNBS)-metmyoglobin adduct formed following the horse metmyoglobin-H 2 O 2 reaction has been assigned to both a tyrosyl and a tryptophanyl residue radical. At low H 2 O 2 , hyperfine coupling to a 1 3 C atom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa7102a016d6e59b48f39b7551a128a6
https://doi.org/10.1021/tx0256580
https://doi.org/10.1021/tx0256580
Publikováno v:
Journal of the American Chemical Society. 123:3412-3417
The pressure stability of the thermophilic CYP119 from Sulfolobus solfataricus and its active-site Thr213 and Thr214 mutants was investigated. At 20 degrees C and pH 6.5, the protein undergoes a reversible P450-to-P420 inactivation with a midpoint at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::81f89554cb4c4bab1ce8c94ba90b094e
https://doi.org/10.1021/ja003947+
https://doi.org/10.1021/ja003947+
Autor:
Laura S. Koo, Richard A. Tschirret-Guth, Thomas M. Loehr, Paul R. Ortiz de Montellano, Wesley E. Straub, Pierre Moënne-Loccoz
Publikováno v:
Journal of Biological Chemistry. 275:14112-14123
CYP119 from Sulfolobus solfataricus, the first thermophilic cytochrome P450, is stable at up to 85 degrees C. UV-visible and resonance Raman show the enzyme is in the low spin state and only modestly shifts to the high spin state at higher temperatur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05f481651812b305bfa9f7f302dc7317
https://doi.org/10.1074/jbc.275.19.14112
https://doi.org/10.1074/jbc.275.19.14112
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 5:204-212
CYP119, the first thermophilic P450 enzyme, reacts much more slowly than CYP101 (P450cam) with aryldiazenes to give sigma-bonded aryl-iron complexes. The CYP119 complexes are stable anaerobically at 80 degrees C but are readily oxidized by O2 to give
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb10d5100b8277573d39639e108e8838
https://doi.org/10.1007/s007750050364
https://doi.org/10.1007/s007750050364
Publikováno v:
Journal of the American Chemical Society. 121:4731-4737
The photoactivatable trifluoromethyldiazirinylphenyldiazene probes 1a and 2a have been synthesized, and their utility in the mapping of hemoprotein active sites has been validated with myoglobin (M...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f80d337daee4b2bb0a52ddb6c7bd412e
https://doi.org/10.1021/ja990351h
https://doi.org/10.1021/ja990351h
Publikováno v:
The Journal of Organic Chemistry. 63:9711-9715
Aryldiazenes with a second, photoactivatable, azide substituent on the aryl ring have been synthesized as active site probes for heme proteins of unknown active site structure. The probes include m...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b2ec731361967460510821d479178ca
https://doi.org/10.1021/jo981095e
https://doi.org/10.1021/jo981095e
Publikováno v:
Journal of the American Chemical Society. 120:7404-7410
The reaction of myoglobin (Mb) with (meta- and (para-azidophenyl)diazene yields the corresponding σ-bonded meta- or para-phenyl−iron complex. Aerobic denaturation of these complexes in the dark yie...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::81022b8cab3178546eaca0a33ac9967e
https://doi.org/10.1021/ja980978k
https://doi.org/10.1021/ja980978k
Publikováno v:
Journal of the American Chemical Society. 120:3590-3596
The reaction of cytochrome P450cam with aryldiazenes (ArNNH) yields σ-bonded iron−aryl (Fe−aryl) complexes. Oxidation of the complexes causes regioselective migration of the aryl group from the iron to the porphyrin nitrogens. The influence of h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::548f07f6a3d77e0926647b17b990d5a4
https://doi.org/10.1021/ja973909z
https://doi.org/10.1021/ja973909z
Autor:
Richard A. Tschirret-Guth, Ronald P. Mason, Janice A. DeGray, Michael R. Gunther, Paul R. Ortiz de Montellano
Publikováno v:
Journal of Biological Chemistry. 272:2359-2362
Globin-centered radicals at tyrosine and tryptophan residues and a peroxyl radical at an unknown location have been reported previously as products of the reaction of metmyoglobin with hydrogen peroxide. The peroxyl radical is shown here to be locali
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e32f0c6a050d3ebdd5060c4001fe811d
https://doi.org/10.1074/jbc.272.4.2359
https://doi.org/10.1074/jbc.272.4.2359