Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Michael T. Wilson"'
Publikováno v:
Archives of biochemistry and biophysics. 554
Kinetic studies using UV/visible and EPR spectroscopy were carried out to follow the distribution of electrons within beef heart cytochrome c oxidase (CcO), both active and cyanide-inhibited, following addition of reduced cytochrome c as electron don
Autor:
Chris E. Cooper, Jason D. Morrow, Victor M. Darley-Usmar, L. Jackson Roberts, Radhi Anand, David Goodier, Michael T. Wilson, Kevin P. Moore, Martine Clozel, Steve Holt, William E. Zackert, Rakesh P. Patel, Brandon J. Reeder, Dimitri A. Svistunenko
Publikováno v:
Journal of Biological Chemistry. 273:31731-31737
Muscle injury (rhabdomyolysis) and subsequent deposition of myoglobin in the kidney causes renal vasoconstriction and renal failure. We tested the hypothesis that myoglobin induces oxidant injury to the kidney and the formation of F2-isoprostanes, po
Publikováno v:
The Biochemical journal. 434(3)
Cytoglobin is a recently discovered hexa-co-ordinate haemoglobin that does not appear to function as a classical oxygen-binding protein. Its function is unknown and studies on the effects of changes in its expression have not decisively determined it
Publikováno v:
Scopus-Elsevier
The Cu(II)-promoted oxidation of lipids is a lipid hydroperoxide (LOOH)-dependent process that has been used routinely to assess the oxidizability of low-density lipoprotein (LDL) in human subjects. Metal-dependent redox reactions, including those me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7f9693acc5b61ccbe21758519be7b88
https://europepmc.org/articles/PMC1218208/
https://europepmc.org/articles/PMC1218208/
Autor:
Jaume Torres, Michael T. Wilson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. (2-3):310-322
Nitric oxide (NO) can act as a ligand for copper atoms and may also engage in redox chemistry with the metal once bound. Furthermore NO posses an unpaired electron which can couple with the unpaired electron on Cu2+. These properties have been exploi
Cytochrome oxidase (EC 1.9.3.1; ferrocytochrome c:oxygen oxidoreductase) was studied during steady-state by optical and e.p.r. methods. Starting with either the ‘resting’ or the ‘pulsed’ enzyme, oxidase, cytochrome c, ascorbate and O2 were mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38e8ead1cef73b8b3aab9dc4551275f1
https://europepmc.org/articles/PMC1158254/
https://europepmc.org/articles/PMC1158254/
Studies on partially reduced mammalian cytochrome oxidase: reactions with carbon monoxide and oxygen
Publikováno v:
Scopus-Elsevier
A number of methods were used to prepare a species of mammalian cytochrome oxidase (EC 1.9.3.1, ferrocytochrome c –oxygen oxidoreductase) in which only cytochrome a 3 is reduced and in combination with CO. The kinetics of CO binding by cytochrome a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ace2aee9ba2ac5c1d77ebe3b8ff42ce
http://www.scopus.com/inward/record.url?eid=2-s2.0-0015954524&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0015954524&partnerID=MN8TOARS