Zobrazeno 21 - 30
of 40
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Bo G. Malmström, Pia Ädelroth, Mikael Sundahl, Pernilla Wittung, Bassam El-Agez, Michael T. Wilson, Peter Brzezinski
Publikováno v:
Biophysical chemistry. 54(2)
The quenching of the triplet state of Zn-cytochrome c in electrostatic complexes with cytochrome oxidase and its soluble CuA domain has been studied by laser flash photolysis. The triplet state of free Zn-cytochrome c decayed with a rate of about 200
Human hemoglobin has been used as a pro-oxidant for artificial unilamellar phospholipid vesicles, containing cytochrome-c oxidase inserted into the bilayer. This experimental system was suitable to follow directly the kinetics of lipid oxidation and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afcdc4a694011aec5012479c840e945f
http://hdl.handle.net/11573/15420
http://hdl.handle.net/11573/15420
Publikováno v:
FEBS letters. 326(1-3)
Peroxynitrite is the product of the reaction between nitric oxide and superoxide. It is an oxidant which can also decompose to form the hydroxyl radical and nitrogen dioxide. In this report we show that a powerful oxidant with reactivity similar to t
Autor:
Mark C Cox, Melanie S. Rogers, Michael T. Wilson, Gareth D. Jones, Andrew J. Thomson, Geoffrey R. Moore, Myles R. Cheesman
Publikováno v:
FEBS letters. 307(2)
A spectroscopic study of the flavocytochrome b enzyme, cellobiose oxidase, employing optical, NMR, EPR and near infra-red MCD techniques, has identified the axial ligands of the b-type haem. These are a histidine and a methionine, and this ligation s
In a recent review article Babcok and Wikstrom (Nature, 1992, 356, 301–309) proposed that the species of cytochrome- c -oxidase which binds molecular oxygen during turnover is the so-called mixed valence enzyme, in which the binuclear center cytoch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ef249da3190f30afe856a8054a54a75
https://hdl.handle.net/11590/132454
https://hdl.handle.net/11590/132454
Autor:
Ralph Beneke, Renate M. Leithauser, Ashril Yusof, Michael T. Wilson, Janice M Conway-Klaassen, Lawrence A. Golding
Publikováno v:
Medicine & Science in Sports & Exercise. 38:S418
Publikováno v:
Biochemical and Biophysical Research Communications. 103:1223-1230
The cysteine residues in beef cytochrome c oxidase (E.C.1.9.3.1) which act as ligands to a redox site have been located in the C-terminal portion of subunit II.
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
Publikováno v:
FEBS Letters. (3):263-266
Previous studies have shown that the addition of nitric oxide to cytochrome c oxidase rapidly generates spectral changes compatible with the formation of nitrite at the binuclear haem:copper centre. Here we directly demonstrate nitrite release follow
Publikováno v:
FEBS Letters. (1):75-78
We have proposed [l] a two-state model to account for the functional properties of cytochrome c oxidase. The basis of the model was the demonstration that the enzyme may exist either in a ‘resting’ (R) or in a ‘pulsed’ (P) state, the two stat