Zobrazeno 1 - 10
of 323
pro vyhledávání: '"Ortiz De Montellano PR"'
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
Publikováno v:
Biochemistry. 39:4684-4691
All parasitic protozoa lack the ability to synthesize purine nucleotides de novo, relying instead on purine salvage enzymes for their survival. Hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT) from the protozoan parasite Tritrichomona
Publikováno v:
Nature Structural Biology. 6:860-867
Heme oxygenase catalyzes the first step in the oxidative degradation of heme. The crystal structure of heme oxygenase-1 (HO-1) reported here reveals a novel helical fold with the heme sandwiched between two helices. The proximal helix provides a heme
Publikováno v:
Biochemistry. 35:12788-12795
The proximal iron ligand in horseradish peroxidase (HRP) is His-170. The H170A mutant of polyhistidine-tagged HRP (hHRP) has been expressed in a baculovirus system and has been purified and characterized. At pH 7, the Soret maximum of the mutant is a
Publikováno v:
Chemical Research in Toxicology. 9:223-226
Cytochrome P450 2E1 (CYP2E1), an enzyme that is induced by ethanol, plays an important role in the metabolism of various toxic and carcinogenic substances, including dialkylnitrosamines and small halocarbons. Little information is available on the ac
Publikováno v:
Chemical Research in Toxicology. 6:38-45
Reaction of cytochrome P450 enzymes with arylacetylenes results in heme N-alkylation [e.g., Komives, E. A., and Ortiz de Montellano, P. R., (1985) J. Biol. Chem. 260, 3330-3336] and/or protein modification [e.g., Gan, L.-S. L., Acebo, A. L. and Alwor
Autor:
Ortiz de Montellano Pr, David P. Barr, Yang C. Fann, Michael R. Gunther, Richard A. Tschirret-Guth, Ronald P. Mason, Witkowska He
The reaction between metmyoglobin and hydrogen peroxide produces both a ferryl-oxo heme and a globin-centred radical(s) from the two oxidizing equivalents of the hydrogen peroxide. Evidence has been presented for localization of the globin-centred ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adc50d36a016176655ed5a0a583ce84e
https://europepmc.org/articles/PMC1219275/
https://europepmc.org/articles/PMC1219275/
Publikováno v:
Biochemistry. 31(35)
Thianthrene 5-oxide (T-5-O), which is oxidized to the 5,10- and 5,5-dioxides, respectively, by electrophilic and nucleophilic agents, has been used to determine the electronic properties of hemoprotein oxidizing species. Cytochrome P450 oxidizes T-5-
Publikováno v:
Natural Product Reports. 24:499
Publikováno v:
Journal of Medicinal Chemistry. 25:1174-1179
The clinically used sedative-hypnotic ethchlorvynol destroys hepatic microsomal cytochrome P-450 enzymes in a process catalyzed by the same hemoproteins. Abnormal porphyrins accumulate in the livers of phenobarbital-pretreated rats after administrati