Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Michael T. Wilson, Brandon J. Reeder
Publikováno v:
Molecular Aspects of Medicine. 84:101045
Under those pathological conditions in which Myoglobin and Hemoglobin escape their cellular environments and are thus separated from cellular reductive/protective systems, the inherent peroxidase activities of these proteins can be expressed. This ac
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:
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:
John S. Olson, Abdu I. Alayash, Wayne Hicks, Tigist Kassa, Michael Brad Strader, Eileen W. Singleton, Michael T. Wilson, Todd L. Mollan, Mitchell J. Weiss, Jayashree Soman
Publikováno v:
Journal of Biological Chemistry. 289:22342-22357
A pathogenic V67M mutation occurs at the E11 helical position within the heme pockets of variant human fetal and adult hemoglobins (Hb). Subsequent post-translational modification of Met to Asp was reported in γ subunits of human fetal Hb Toms River
Publikováno v:
Journal of Biological Chemistry. 285:19785-19792
Mammalian mitochondrial cytochrome c interacts with cardiolipin to form a complex (cyt. c/CL) important in apoptosis. Here we show that this interaction leads to structural changes in ferrocytochrome c that leads to an open coordinate site on the cen
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:
Journal of Biological Chemistry. 282:1638-1649
Substitution of the heme coordination residue Met-80 of the electron transport protein yeast iso-1-cytochrome c allows external ligands like CO to bind and thus increase the effective redox potential. This mutation, in principle, turns the protein in
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:
Nitric Oxide. 27:S24
The production of nitric oxide by the nitrite reductase activity of deoxyhemoglobin has been proposed to play a major role in hypoxic vasodilation. A feature of this mechanism is that deoxyhemoglobin sites in the R state of tetrameric hemoglobin favo
Autor:
M.M.M. Saleem, Michael T. Wilson
Publikováno v:
Inorganica Chimica Acta. 153:105-113
The temperature dependency of ligand binding processes lend support to the proposed mechanisms and the factors affecting ligand binding reported earlier in this series. The free energy contribution from each factor affecting ligand binding was estima