Zobrazeno 1 - 10 of 243 pro vyhledávání: '"MINOR J. COON"'
1
Peroxidase-like activity of uncoupled cytochrome P450
Autor: Donovan C. Haines, Minor J. Coon, Ronald W. Estabrook, Francesco De Matteis, David P. Ballou
Publikováno v: Biochemical Pharmacology. 84:374-382
The NADPH-dependent consumption of O(2) by cytochrome P450 BM3 was stimulated by either laurate or perfluorolaurate, but the NADPH/O(2) molar consumption ratios were approximately 1 and 2, respectively, indicating that perfluorolaurate does not becom
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6e0e51dacdaf5a70343bb48fcf7ab8f8
https://doi.org/10.1016/j.bcp.2012.04.016
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2
Products from Enzyme-Catalyzed Oxidations of Norcarenes
Autor: Stephen J. Lippard, Paul F. Hollenberg, Minor J. Coon, Leslie J. Murray, R. Esala P. Chandrasena, Viviana Izzo, Dharmika S.P. Lansakara-P, Martin Newcomb, Hye Yeong Kim, Laurance G. Beauvais
Publikováno v: The Journal of Organic Chemistry. 72:1128-1133
Recent studies revealed that norcarane (bicyclo[4.1.0]heptane) is oxidized to 2-norcarene (bicyclo[4.1.0]-hept-2-ene) and 3-norcarene (bicyclo[4.1.0]hept-3-ene) by iron-containing enzymes and that secondary oxidation products from the norcarenes comp
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8964692ed3cb88d22a5b0a9c1a08fffd
https://doi.org/10.1021/jo061865j
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3
Abolition of oxygenase function, retention of NADPH oxidase activity, and emergence of peroxidase activity upon replacement of the axial cysteine-436 ligand by histidine in cytochrome P450 2B4
Autor: Kostas P. Vatsis, Hwei Ming Peng, Minor J. Coon
Publikováno v: Archives of Biochemistry and Biophysics. 434:128-138
A fundamental aspect of cytochrome P450 function is the role of the strictly conserved axial cysteine ligand, replacement of which by histidine has invariably resulted in mammalian and bacterial preparations devoid of heme. Isolation of the His-436 v
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::743c1443a5ea9639a79f4b1c9968b551
https://doi.org/10.1016/j.abb.2004.10.015
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6
Cytochrome P450, a very hard mountain to climb: evidence for multiple functional species of activated oxygen
Autor: Minor J. Coon, Hwei Ming Peng, Kostas P. Vatsis
Publikováno v: International Congress Series. 1233:487-493
Although much has been learned about cytochrome P450 as an oxygenating catalyst since its discovery as a carbon monoxide-binding pigment in liver microsomes over 40 years ago, two major problems remain unsolved. These are the role of the heme sulfur
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d6244b4c3a8d5f6b2acbb313c2869999
https://doi.org/10.1016/s0531-5131(02)00281-9
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7
Replacement of active-site cysteine-436 by serine converts cytochrome P450 2B4 into an NADPH oxidase with negligible monooxygenase activity
Autor: Hwei Ming Peng, Minor J. Coon, Kostas P. Vatsis
Publikováno v: Journal of Inorganic Biochemistry. 91:542-553
The function of the unique axial thiolate ligand of cytochrome P450 has been investigated by mutagenesis of the active-site cysteine with other amino acids in NH(2)-truncated P450s 2B4 and 2E1. The expressed Ser-436 variant of P450 2B4 was highly pur
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8162e956de7ada1164e24bab05bb7745
https://doi.org/10.1016/s0162-0134(02)00438-5
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8
Ipso-Substitution by Cytochrome P450 with Conversion of p-Hydroxybenzene Derivatives to Hydroquinone: Evidence for Hydroperoxo-Iron As the Active Oxygen Species
Autor: Minor J. Coon, Kostas P. Vatsis
Publikováno v: Archives of Biochemistry and Biophysics. 397:119-129
Evidence for multiple functional active oxidants in cytochrome P450-catalyzed reactions was previously obtained in this laboratory with mutants in which proton delivery was perturbed by replacement of the highly conserved threonine residue in the act
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdf9ecd11e0fa0831f142179d63da8b9
https://doi.org/10.1006/abbi.2001.2665
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9
Cytochrome P450-Catalyzed Hydroxylation of Mechanistic Probes that Distinguish between Radicals and Cations. Evidence for Cationic but Not for Radical Intermediates
Autor: Seung-Yong Choi, Paul F. Hollenberg, Martin Newcomb, Minor J. Coon, Patrick H. Toy, Runnan Shen, Alfin D. N. Vaz
Publikováno v: Journal of the American Chemical Society. 122:2677-2686
Oxidation of the mechanistic probes trans,trans-2-methoxy-3-phenylmethylcyclopropane and methylcubane by six cytochrome P450 isozymes has been studied. The probes differentiate between radical and cationic species in that different structural rearran
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::36e0eb566f7483bab342aff14d9c6846
https://doi.org/10.1021/ja994106+
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10
Epoxidation of olefins by cytochrome P450: Evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant
Autor: Dermot F. Mcginnity, Minor J. Coon, Alfin D. N. Vaz
Publikováno v: Proceedings of the National Academy of Sciences. 95:3555-3560
P450 cytochromes (P450) catalyze many types of oxidative reactions, including the conversion of olefinic substrates to epoxides by oxygen insertion. In some instances epoxidation leads to the formation of products of physiological importance from nat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c780337a7ee2e8ca84ba45b1a2b8b20
https://doi.org/10.1073/pnas.95.7.3555
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