Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Dimitri A. Svistunenko, Jonathan A. R. Worrall, Michael T. Wilson, Robin L. Owen, Marina Lučić, Michael A. Hough
Publikováno v:
Journal of Biological Inorganic Chemistry
Structure determination of proteins and enzymes by X-ray crystallography remains the most widely used approach to complement functional and mechanistic studies. Capturing the structures of intact redox states in metalloenzymes is critical for assigni
Publikováno v:
Chemistry – A European Journal. 25:10678-10688
The chemical basis for protecting organisms against the toxic effect imposed by excess cuprous ions is to constrain this through high-affinity binding sites that use cuprous-thiolate coordination chemistry. In bacteria, a family of cysteine rich four
Publikováno v:
Free Radical Biology & Medicine
Covalent hemoglobin binding to membranes leads to band 3 (AE1) clustering and the removal of erythrocytes from the circulation; it is also implicated in blood storage lesions. Damaged hemoglobin, with the heme being in a redox and oxygen-binding inac
Autor:
Jonathan A. R. Worrall, Michael A. Hough, Tadeo Moreno Chicano, Amanda K. Chaplin, Dimitri A. Svistunenko, Bethany V. Hampshire, Michael T. Wilson
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 25(24)
Dye decolouring peroxidases (DyPs) are the most recent class of heme peroxidase to be discovered. On reacting with H2 O2 , DyPs form a high-valent iron(IV)-oxo species and a porphyrin radical (Compound I) followed by stepwise oxidation of an organic
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:
Michael T. Wilson, Robert C. Hider, Francesca Cutruzzolà, Brandon J. Reeder, Maria Giulia Bigotti
Publikováno v:
Free Radical Biology and Medicine. 44:274-283
A wide range of organic reductants, including many iron chelators, reduce ferryl myoglobin to its ferric states in exponential time courses whose rate constants display double hyperbolic dependencies on the reductant concentration. This concentration
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
Publikováno v:
Journal of Inorganic Biochemistry. 66:207-212
The effect of the free radical nitric oxide (NO) on the activity of isolated cytochrome sigma oxidase was investigated by using ferrocytochrome sigma as an electron donor, and the system SNOG/DTT, which produces a steady-state NO concentration simila
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