Zobrazeno 1 - 10
of 117
pro vyhledávání: '"O Einarsdóttir"'
Autor:
R A Goldbeck, D S Kliger, O Einarsdóttir, William H. Woodruff, S J Atherton, G Palmer, T D Dawes, R.B. Dyer, Kimberly A. Bagley
Publikováno v:
Proceedings of the National Academy of Sciences. 88:2588-2592
Time-resolved electronic absorption, infrared, resonance Raman, and magnetic circular dichroism spectroscopies are applied to characterization of the intermediate that is formed within 20 ps after photodissociation of CO from cytochrome a3 in reduced
Publikováno v:
European journal of biochemistry. 267(18)
A novel method for initiating intramolecular electron transfer in cytochrome c oxidase is reported. The method is based upon photoreduction of cytochrome c labeled with thiouredopyrene-3,6, 8-trisulfonate in complex with cytochrome oxidase. The thiou
Autor:
B M Hoffman, William E. Antholine, R B Dyer, R J Gurbiel, W H Woodruff, K K Surerus, J A Fee, C Fan, O Einarsdóttir, W A Oertling
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 89(8)
Cytochrome ba3 from Thermus thermophilus reacts slowly with excess HCN at pH 7.4 to create a form of the enzyme in which CuA, cytochrome b, and CuB remain oxidized, while cytochrome a3 is reduced by one electron, presumably with the formation of cyan
Akademický článek
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Autor:
Winslow S. Caughey, O Einarsdóttir
Publikováno v:
Journal of Biological Chemistry. 263:9199-9205
The interactions of nitrous oxide with cytochrome c oxidase isolated from bovine heart muscle have been investigated in search of an explanation for the inhibition of mitochondrial respiration by the inhalation anesthetic. Oxidase activity of the iso
Publikováno v:
Journal of Biological Chemistry. 264:2405-2408
The C-O stretching frequencies of fully reduced carbonmonoxy cytochrome ba3, a newly discovered terminal oxidase of the bacterium Thermus thermophilus (Zimmermann, B.H., Nitsche, C.I., Fee, J.A., Rusnak, F., and Munck, E. (1988) Proc. Natl. Acad. Sci
Publikováno v:
Journal of Biological Chemistry. 263:13641-13654
The site and mechanism of dioxygen reduction in cytochrome c oxidase from bovine heart muscle have been investigated. The rate of cytochrome c2+ oxidation by O2 is shown to be affected by several factors: 1) pH, with optima at 5.65 and 6.0, 2) temper
Akademický článek
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Publikováno v:
The Journal of biological chemistry. 263(27)
The site and mechanism of dioxygen reduction in cytochrome c oxidase from bovine heart muscle have been investigated. The rate of cytochrome c2+ oxidation by O2 is shown to be affected by several factors: 1) pH, with optima at 5.65 and 6.0, 2) temper
Autor:
O, Einarsdóttir, W S, Caughey
Publikováno v:
The Journal of biological chemistry. 263(19)
The interactions of nitrous oxide with cytochrome c oxidase isolated from bovine heart muscle have been investigated in search of an explanation for the inhibition of mitochondrial respiration by the inhalation anesthetic. Oxidase activity of the iso