Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Richard W. White, Michael T. Wilson, Jonathan A. R. Worrall, Geoffrey R. Moore, Oliver M. Deacon
Publikováno v:
Journal of Inorganic Biochemistry. 203:110924
Mitochondrial cytochrome c is associated with electron transfer in the respiratory chain and in apoptosis. Four cytochrome c variants have been identified in families that suffer from mild autosomal dominant thrombocytopenia, a platelet disorder asso
Autor:
Amanda K. Chaplin, Jonathan A. R. Worrall, Erik Vijgenboom, Vassiliy N. Bavro, Michael T. Wilson, Jordi Paps, Michael A. Hough, Megan L. Straw
Publikováno v:
Metallomics, 10(1), 180-193. OXFORD UNIV PRESS
Metallomics
Metallomics
Streptomyces lividans has a distinct dependence on the bioavailability of copper for its morphological development. A cytosolic copper resistance system is operative in S. lividans that serves to preclude deleterious copper levels. This system compri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::681a7d249fbab6f8edf28b9258389ed7
http://hdl.handle.net/1887/3217486
http://hdl.handle.net/1887/3217486
Autor:
Paolo Ascenzi, Michael T. Wilson, Fabio Polticelli, Laura Fiorucci, Roberto Santucci, Maria Marino, Massimo Coletta, Federica Sinibaldi
Publikováno v:
IUBMB Life. 67:98-109
Cytochrome c (cytc) is a small heme-protein located in the space between the inner and the outer membrane of the mitochondrion that transfers electrons from cytc-reductase to cytc-oxidase. The hexa-coordinated heme-Fe atom of cytc displays a very low
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
Publikováno v:
Journal of the American Chemical Society. 134:7741-7749
Tyrosine residues can act as redox cofactors that provide an electron transfer ("hole-hopping") route that enhances the rate of ferryl heme iron reduction by externally added reductants, for example, ascorbate. Aplysia fasciata myoglobin, having no n
Autor:
Andreas Ioannis Karsisiotis, Jonathan A. R. Worrall, Colin J. Macdonald, Oliver M. Deacon, Michael T. Wilson, Tharin M. A. Blumenschein, Geoffrey R. Moore
Publikováno v:
Biophysical Journal. 112:32a-33a
In addition to its well-known role as a component of the electron transport chain, mitochondrial cytochrome c can also act as a peroxidase in the early stages of the intrinsic apoptosis pathway. Ferricytochrome c contains a hexacoordinated heme iron,
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:
Biophysical Chemistry. 98:65-77
The iron ligand, Met80, of yeast iso-1-cytochrome c has been mutated to residues that are unable to bind to the iron. The resultant proteins, Met80Ala, Ser, Asp, Glu, have been expressed and purified. All mutant proteins exhibit well defined pH depen
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:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1364(3):385-389
Photoinduced electron transfer from cytochrome c to plastocyanin was investigated using a novel method. Reduced carboxymethylated cytochrome c (CmCyt c), with carbon monoxide bound to the heme iron, and oxidized plastocyanin were mixed. At 1 mM CO th