Zobrazeno 1 - 10
of 27
pro vyhledávání: '"F M, Raushel"'
Publikováno v:
Electrophoresis. 21(15)
The capillary electrophoretic separation of noncharged enantiomers with single-isomer anionic resolving agents is reexamined here with the help of the charged resolving agent migration model. Two general model parameters have been identified that inf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::751a02f2ebb076f84bf51b619a06b28e
https://pubmed.ncbi.nlm.nih.gov/11001223
https://pubmed.ncbi.nlm.nih.gov/11001223
Autor:
F M, Raushel, H M, Holden
Publikováno v:
Advances in enzymology and related areas of molecular biology. 74
The bacterial PTE is able to catalyze the hydrolysis of a wide range of organophosphate nerve agents. The active site has been shown to consist of a unique binuclear metal center that has evolved to deliver hydroxide to the site of bond cleavage. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7ae1bf4acb66e9fd3e6c7b90b28116f8
https://pubmed.ncbi.nlm.nih.gov/10800593
https://pubmed.ncbi.nlm.nih.gov/10800593
Publikováno v:
Proteins. 29(4)
Phosphotriesterase (PTE) is a zinc metalloenzyme that catalyzes the hydrolysis of an extensive array of organophosphate pesticides and mammalian acetylcholinesterase nerve agents. Although the three-dimensional crystal structure of PTE has been solve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7f8348bb4aa91c755017869cbee7fbce
https://pubmed.ncbi.nlm.nih.gov/9408951
https://pubmed.ncbi.nlm.nih.gov/9408951
Publikováno v:
The Journal of biological chemistry. 272(28)
Nitric oxide synthases (NOS) are hemeproteins that catalyze oxidation of L-arginine to nitric oxide (NO) and citrulline. The NOS heme iron is expected to participate in oxygen activation during catalysis, but its interactions with O2 are not characte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::be01cf4ebcf4839a2023e7c372d6ebb0
https://pubmed.ncbi.nlm.nih.gov/9211873
https://pubmed.ncbi.nlm.nih.gov/9211873
Publikováno v:
Protein science : a publication of the Protein Society. 5(2)
Ribonuclease T1 (RNase T1) is a small, globular protein of 104 amino acids for which extensive thermodynamic and structural information is known. To assess the specific influence of variations in amino acid sequence on the mechanism for protein foldi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::87f2076fb834424059f679ecce5b76b2
https://pubmed.ncbi.nlm.nih.gov/8745397
https://pubmed.ncbi.nlm.nih.gov/8745397
Autor:
L S Mullins, F M Raushel
The positional isotope exchange technique has been found to be quite useful for the identification of reaction intermediates in enzyme-catalyzed reactions. For reactions where intermediates are not expected the method can be used with great utility f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c565f4537fccbe3217d5f57bd383c445
https://doi.org/10.1016/0076-6879(95)49043-4
https://doi.org/10.1016/0076-6879(95)49043-4
Autor:
L S, Mullins, F M, Raushel
Publikováno v:
Methods in enzymology. 249
The positional isotope exchange technique has been found to be quite useful for the identification of reaction intermediates in enzyme-catalyzed reactions. For reactions where intermediates are not expected the method can be used with great utility f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7405edbc8bc4b404f56e5448fad18884
https://pubmed.ncbi.nlm.nih.gov/7791621
https://pubmed.ncbi.nlm.nih.gov/7791621
Publikováno v:
The Journal of biological chemistry. 268(33)
Bacterial luciferase catalyzes the reaction of FMNH2, O2, and an aliphatic aldehyde to yield the carboxylic acid, FMN, water and blue-green light. The kinetics of the bacterial luciferase reaction were measured by stopped-flow spectrophotometry at pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e463b46cce569d5d19f2834a5fb06806
https://pubmed.ncbi.nlm.nih.gov/8227032
https://pubmed.ncbi.nlm.nih.gov/8227032
Publikováno v:
The Journal of biological chemistry. 268(11)
Bacterial luciferase catalyzes the formation of visible light, FMN, and a carboxylic acid from FMNH2, O2, and the corresponding aldehyde. The reactive cysteinyl residue at position 106 of the alpha subunit has been replaced by serine, alanine, and va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7d8b067a691ef5f3928a5b577bd6e297
https://pubmed.ncbi.nlm.nih.gov/8463299
https://pubmed.ncbi.nlm.nih.gov/8463299
Publikováno v:
The Journal of biological chemistry. 267(19)
The bacterial phosphotriesterase has been found to require a divalent cation for enzymatic activity. This enzyme catalyzes the detoxification of organophosphorus insecticides and nerve agents. In an Escherichia coli expression system significantly hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::15aa0811e23264dae455a8b2482e244b
https://pubmed.ncbi.nlm.nih.gov/1320014
https://pubmed.ncbi.nlm.nih.gov/1320014