Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Gary Silkstone, Badri S. Rajagopal, Michael T. Wilson, Peter Nicholls, Jonathan A. R. Worrall
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817:780-791
Mitochondrial cytochrome c associates with the phosphoplipid cardiolipin (CL) through a combination of electrostatic and hydrophobic interactions. The latter occurs by insertion into cytochrome c of an acyl chain, resulting in the dissociation of the
Autor:
Ursula Liebl, Michael T. Wilson, Latifa Bouzhir-Sima, Marten H. Vos, Taku Yamashita, Laura Lobato
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (38), pp.26514-24. ⟨10.1074/jbc.M114.571398⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (38), pp.26514-24. ⟨10.1074/jbc.M114.571398⟩
International audience; DNR (dissimilative nitrate respiration regulator) is a heme-binding transcription factor that is involved in the regulation of denitrification in Pseudomonas aeruginosa. In the ferrous deoxy state, the heme is 6-coordinate; ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::950f1d704309843293227820feb66809
https://hal-polytechnique.archives-ouvertes.fr/hal-01079002
https://hal-polytechnique.archives-ouvertes.fr/hal-01079002
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
Publikováno v:
Nitric oxide : biology and chemistry. 35
The production of nitric oxide by hemoglobin (Hb) has been proposed to play a major role in the control of blood flow. Because of the allosteric nature of hemoglobin, the nitrite reductase activity is a complex function of oxygen partial pressure PO2
Publikováno v:
Nitric oxide : biology and chemistry. 33
The production of nitric oxide by the nitrite reductase activity of hemoglobin has been proposed to play a major role in hypoxic vasodilation. The bimolecular reaction rate constant for nitric oxide formation is a complex function of hemoglobin oxyge
Publikováno v:
Biochemistry. 51(34)
Cardiolipin, a phospholipid specific to the mitochondrion, interacts with the small electron transfer heme protein cytochrome c through both electrostatic and hydrophobic interactions. Once in a complex with cardiolipin, cytochrome c has been shown t
Autor:
Brandon J, Reeder, Marie, Grey, Radu-Lucian, Silaghi-Dumitrescu, Dimitri A, Svistunenko, Leif, Bülow, Chris E, Cooper, Michael T, Wilson
Publikováno v:
The Journal of biological chemistry. 283(45)
Respiratory proteins such as myoglobin and hemoglobin can, under oxidative conditions, form ferryl heme iron and protein-based free radicals. Ferryl myoglobin can safely be returned to the ferric oxidation state by electron donation from exogenous re
Autor:
Michael T. Wilson, Radu Silaghi-Dumitrescu, Francesca Cutruzzolà, Serena Rinaldo, Chris E. Cooper, Brandon J. Reeder, Mieebi M. Wankasi, Dimitri A. Svistunenko
Publikováno v:
Dalton transactions (Cambridge, England : 2003). (8)
Myoglobin (Mb) from gastropod mollusc Aplysia limacina shows only 20% sequence homology to the ‘prototype’ sperm whale Mb but exhibits a typical Mb fold and can reversibly bind oxygen. An intriguing feature of aplysia Mb is that it lacks the dist
Autor:
Beth R, Cameron, Marilyn C, Darkes, Helen, Yee, Micki, Olsen, Simon P, Fricker, Renato T, Skerlj, Gary J, Bridger, Nathan A, Davies, Michael T, Wilson, David J, Rose, Jon, Zubieta
Publikováno v:
Inorganic chemistry. 42(6)
The preparation of two Ru(III) polyaminocarboxylate complexes, AMD6245 and AMD6221, and their nitrosyl analogues, AMD6204, AMD6263, and AMD3689, is described. The compounds are characterized by IR, ES-MS, and (13)C and (15)N NMR spectroscopy where ap
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