Zobrazeno 1 - 10 of 32 pro vyhledávání: '"H J, Bright"'
3
3-Carbanionic substrate analogues bind very tightly to fumarase and aspartase
Autor: H J Bright, D J Porter
Publikováno v: Journal of Biological Chemistry. 255:4772-4780
We describe the interactions at 25 degrees C of the 3-carbanions (I-) and 3-carbon conjugate acids (I) of 3-nitropropionate, 3-nitro-2-hydroxypropionate, and 3-nitro-2-aminopropionate with fumarase and aspartase. (Formula: see text) 1. Ia- and Ib- in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2b70fd53fbc2f355cabbf37abefd854c
https://doi.org/10.1016/s0021-9258(19)85564-3
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4
The mechanism of oxidation of nitroalkanes by horseradish peroxidase
Autor: H J Bright, D J Porter
Publikováno v: Journal of Biological Chemistry. 258:9913-9924
Horseradish peroxidase catalyzes the anaerobic oxidation of 2-nitropropane (probably as the nitronate R-) by H2O2 via Compounds I and II to form R-R. The oxidation rate is stimulated 10-fold by O2 and the products become acetone and NO-2. The aerobic
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3a660527bb593d790543425f6bf55535
https://doi.org/10.1016/s0021-9258(17)44585-6
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5
Active site chlorination of D-amino acid oxidase by N-chloro-D-leucine
Autor: D J Porter, H J Bright
Publikováno v: Journal of Biological Chemistry. 251:6150-6153
N-Chloro-D-leucine is an irreversible inhibitor or D-amino acid oxidase on a time scale of seconds. Studies with N-[36C]chloro-D-leucine, N-chloro-D-[1-14C]leucine and N-chloro-D-[4,5-3H]leucine show that the modified enzyme has been chlorinated at a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2b471d5d6972a99515ff0c866ee150e3
https://doi.org/10.1016/s0021-9258(17)33072-7
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7
The cyanogenic substrate for horseradish peroxidase is a conjugated enamine
Autor: D. J. T. Porter, H. J. Bright
Publikováno v: Journal of Biological Chemistry. 262:9154-9159
We identify the cyanogenic substrate for horseradish peroxidase (HRP) as a conjugated enamine and explore this unusual reaction using alpha-aminocinnamate (RH) as follows. 1) HRP catalyzes the oxidation of RH by O2 (and its peroxidation by H2O2 to fo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::97d71d6aacc61b709778a6cee662d4b7
https://doi.org/10.1016/s0021-9258(18)48061-1
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9
Ethanenitronate is a peroxide-dependent suicide substrate for catalase
Autor: H. J. Bright, D. J. T. Porter
Publikováno v: Journal of Biological Chemistry. 262:9608-9614
We find ethanenitronate (formula; see text) to be a H2O2- (and peracetic acid-) dependent suicide substrate for bovine liver catalase (E) which converts E to Em, a modified form of the enzyme. The catalytic and suicide pathways are related to E, Em,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ff576f51cad92ed2f88d94c386a9282b
https://doi.org/10.1016/s0021-9258(18)47977-x
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10
3-Carbanionic substrate analogues bind very tightly to fumarase and aspartase
Autor: D J, Porter, H J, Bright
Publikováno v: The Journal of biological chemistry. 255(10)
We describe the interactions at 25 degrees C of the 3-carbanions (I-) and 3-carbon conjugate acids (I) of 3-nitropropionate, 3-nitro-2-hydroxypropionate, and 3-nitro-2-aminopropionate with fumarase and aspartase. (Formula: see text) 1. Ia- and Ib- in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b62487e41a59029daa4c492e6be28f5e
https://pubmed.ncbi.nlm.nih.gov/7372610
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