Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Michael T. Wilson, Asma Munir, Steven W. Hardwick, Dimitri Y. Chirgadze, Amanda K. Chaplin, Jonathan A. R. Worrall, Tom L. Blundell
Publikováno v:
Structure(London, England:1993)
Summary Resolution advances in cryoelectron microscopy (cryo-EM) now offer the possibility to visualize structural effects of naturally occurring resistance mutations in proteins and also of understanding the binding mechanisms of small drug molecule
Publikováno v:
Enzyme and Microbial Technology. 25:38-47
The production of extracellular lignocellulose-degrading enzymes, endo-1,4-β-xylanase, endo-1,4-β-glucanase and peroxidase during the growth of Thermomonospora fusca BD25 in basal salts-yeast extract medium containing different carbon sources was s
Publikováno v:
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 115:421-428
Cytochrome c oxidases were isolated from heart tissue of beef ( Bos tauros ), sheep ( Ovis aries ), horse ( Equus caballus ), pig ( Sus scrofa ) (native dimers) and hammerhead shark ( Sphyrna lewinii ) (native monomer). Limited proteolysis of dimeric
Autor:
Michael J. Osborne, Graham S. Bailey, Geoffrey R. Moore, Michael T. Wilson, Talal S. El-Thaher
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1160:235-238
The 1H-NMR spectra have been obtained for rat submandibular kallikrein in the absence and presence of inhibitors. Two competitive inhibitors were investigated, the tripeptide leupeptin (a potent inhibitor with Ki 0.5 microM) and a hexapeptide (a much
Publikováno v:
Nitric Oxide. 27:S11-S12
Mitochondrial cytochrome c oxidase (CCO) is responsible for >95% of mammalian oxygen consumption, and is key to generation of the electrochemical proton gradient required for the bulk of ATP production. Nitric oxide (NO) is a signalling molecule with
Autor:
Brandon J. Reeder, Michael T. Wilson, Gary Silkstone, Andrew S. Ball, Peter Nicholls, Maria G. Mason
Actinomycetes secrete into their surroundings a suite of enzymes involved in the biodegradation of plant lignocellulose; these have been reported to include both hydrolytic and oxidative enzymes, including peroxidases. Reports of secreted peroxidases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::678d179bb052475165cf9253d13c6582
https://europepmc.org/articles/PMC93197/
https://europepmc.org/articles/PMC93197/
Publikováno v:
Enzyme and microbial technology. 29(1)
Streptomyces albus ATCC 3005 was found to produce higher levels of extracellular peroxidase activity (3.420 U mg(-1)) than previously reported for any other actinomycete. Maximum peroxidase activity was obtained after 72 h of incubation at a temperat
Autor:
Abdul Rob, Andrew S. Ball, Martyn C. R. Symons, Jaume Torres, Dimitri A. Svistunenko, Michael T. Wilson, Chris E. Cooper
Publikováno v:
Biochimica et biophysica acta. 1434(1)
The actinomycete Thermomonospora fusca BD25 contains a peroxidase with a high activity over a broad range of temperature and pH and a high stability against denaturing agents. Unusually this peroxidase (PO) is a non-haem enzyme. As prepared PO is cha
Autor:
Maurizio Brunori, Jaume Torres, Michael T. Wilson, Paolo Sarti, Gottfried Stubauer, Alessandro Giuffrè
Publikováno v:
The Journal of biological chemistry
273 (1998): 32475–32478. doi:10.1074/jbc.273.49.32475
info:cnr-pdr/source/autori:Giuffrè A, Stubauer G, Brunori M, Sarti P, Torres J, Wilson MT/titolo:Chloride bound to oxidized cytochrome c oxidase controls the reaction with nitric oxide/doi:10.1074%2Fjbc.273.49.32475/rivista:The Journal of biological chemistry (Print)/anno:1998/pagina_da:32475/pagina_a:32478/intervallo_pagine:32475–32478/volume:273
273 (1998): 32475–32478. doi:10.1074/jbc.273.49.32475
info:cnr-pdr/source/autori:Giuffrè A, Stubauer G, Brunori M, Sarti P, Torres J, Wilson MT/titolo:Chloride bound to oxidized cytochrome c oxidase controls the reaction with nitric oxide/doi:10.1074%2Fjbc.273.49.32475/rivista:The Journal of biological chemistry (Print)/anno:1998/pagina_da:32475/pagina_a:32478/intervallo_pagine:32475–32478/volume:273
The reaction of nitric oxide (NO) with oxidized fast cytochrome c oxidase was investigated by stopped-flow, amperometry, and EPR, using the enzyme as prepared or after "pulsing." A rapid reduction of cytochrome a is observed with the pulsed, but not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::617440ceb57ec2c21fa8e490e8e57074
http://www.scopus.com/inward/record.url?eid=2-s2.0-0032484222&partnerID=40&md5=e54ad531f9e87b1c65d693446dd53e44
http://www.scopus.com/inward/record.url?eid=2-s2.0-0032484222&partnerID=40&md5=e54ad531f9e87b1c65d693446dd53e44
Publikováno v:
Biochemistry. 35(22)
We have used stopped-flow rapid reaction methods, employing both fluorescence and absorbance monitoring, together with HPLC analysis of the products to study the activation of soybean 15-lipoxygenase by 13(S)-hydroperoxy-9, 11(E,Z)-octadecadienoic ac