Zobrazeno 1 - 9
of 9
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
Publikováno v:
Biochimica et biophysica acta. 1655(1-3)
It has been reported that different amino acid radicals are formed following the addition of hydrogen peroxide to cytochrome c oxidase (CcO) from bovine heart or from Paracoccus denitrificans. A broad unresolved signal in the electron paramagnetic re
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 142(2)
A new method of EPR spectral analysis is developed to quantitate overlapping signals. The method requires double integration of a number of spectra containing the signals in different proportions and the subsequent solution of a system of linear equa
Autor:
Abdul Rob, Andrew S. Ball, Martyn C. R. Symons, Jaume Torres, Dimitri A. Svistunenko, Michael T. Wilson, Chris E. Cooper
Publikováno v:
Biochimica et biophysica acta. 1434(1)
The actinomycete Thermomonospora fusca BD25 contains a peroxidase with a high activity over a broad range of temperature and pH and a high stability against denaturing agents. Unusually this peroxidase (PO) is a non-haem enzyme. As prepared PO is cha
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
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
Autor:
Michael J. Fryer, Michael T. Wilson, Brandon J. Reeder, Dimitri A. Svistunenko, Peter Nicholls, Jacqueline Dunne, Chris E. Cooper, Francesca Cutruzzolà, Maria Giulia Bigotti
Publikováno v:
Biophysical Journal. (5):2845-2855
The reactions of hydrogen peroxide with human methemoglobin, sperm whale metmyoglobin, and horse heart metmyoglobin were studied by electron paramagnetic resonance (EPR) spectroscopy at 10 K and room temperature. The singlet EPR signal, one of the th
Autor:
John R. Guest, Simon C. Andrews, Michael T. Wilson, Pauline M. Harrison, Andrew J. Thomson, Nick E. Le Brun, Geoffrey R. Moore
Publikováno v:
FEBS Letters. (1-2):197-202
The mechanism by which iron-storage proteins take up and oxidise iron(II) is not understood. We show by rapid-kinetic and EPR measurements that iron uptake, in vitro, by a bacterial iron-storage protein, bacterioferritin, involves at least three kine
Publikováno v:
FEBS Letters. (1-3):29-32
We have used optical and electron paramagnetic spectroscopy to study the flavohaem enzyme cellobiose oxidoreductase (CBOR) from Phanerochaete chrysosporium. We have examined redox cycles of the enzyme in which the oxidation of cellobiose to cellobion