Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Hiroshi Sugimoto, Takehiko Tosha, Ivo Tews, Robin L. Owen, A. Ebrahim, Michael A. Hough, Amanda K. Chaplin, Michael T. Wilson, Bradley Davy, Shigeki Owada, Dimitri A. Svistunenko, Florian S. N. Dworkowski, Marina Lučić, Jonathan A. R. Worrall, Danny Axford
Publikováno v:
Angewandte Chemie (International Ed. in English)
Obtaining structures of intact redox states of metal centers derived from zero dose X‐ray crystallography can advance our mechanistic understanding of metalloenzymes. In dye‐decolorising heme peroxidases (DyPs), controversy exists regarding the m
Autor:
Michael T. Wilson, Asma Munir, Steven W. Hardwick, Dimitri Y. Chirgadze, Amanda K. Chaplin, Jonathan A. R. Worrall, Tom L. Blundell
Publikováno v:
Structure(London, England:1993)
Summary Resolution advances in cryoelectron microscopy (cryo-EM) now offer the possibility to visualize structural effects of naturally occurring resistance mutations in proteins and also of understanding the binding mechanisms of small drug molecule
Autor:
Michael T. Wilson, Geoffrey R. Moore, Jonathan A. R. Worrall, Oliver M. Deacon, Dimitri A. Svistunenko
Publikováno v:
Biochemistry. 57(29)
Naturally occurring mutations found in one of the two Ω-loop substructures in human cytochrome c are associated with low blood platelet count (thrombocytopenia). Both Ω-loops participate in the formation of conformers associated with cytochrome c p
Autor:
Michael T. Wilson, Andreas Ioannis Karsisiotis, Colin J. Macdonald, Tharin M. A. Blumenschein, Geoffrey R. Moore, Oliver M. Deacon, Jonathan A. R. Worrall
Publikováno v:
Scientific Reports
Thrombocytopenia 4 is an inherited autosomal dominant thrombocytopenia, which occurs due to mutations in the human gene for cytochrome c that results in enhanced mitochondrial apoptotic activity. The Gly41Ser mutation was the first to be reported. He
Publikováno v:
Journal of the American Chemical Society. 134:7741-7749
Tyrosine residues can act as redox cofactors that provide an electron transfer ("hole-hopping") route that enhances the rate of ferryl heme iron reduction by externally added reductants, for example, ascorbate. Aplysia fasciata myoglobin, having no n
Autor:
Michael Brad, Strader, Wayne A, Hicks, Tigist, Kassa, Eileen, Singleton, Jayashree, Soman, John S, Olson, Mitchell J, Weiss, Todd L, Mollan, Michael T, Wilson, Abdu I, Alayash
Publikováno v:
The Journal of biological chemistry. 289(32)
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
Autor:
Jonathan A. R. Worrall, Christopher J. Howe, Michael T. Wilson, Derek S. Bendall, Badri S. Rajagopal
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 16(4)
The amino acid at position 51 in the cytochrome c 6 family is responsible for modulating over 100 mV of heme midpoint redox potential. As part of the present work, the X-ray structure of the imidazole adduct of the photosynthetic cytochrome c 6 Q51V
Publikováno v:
Journal of the American Chemical Society. 127(1)
The ferric forms of Met80X mutants of yeast iso-1-cytochrome c (X = Ala, Ser, Asp, and Glu) display EPR and optical spectra that are strongly pH dependent. At low pH values (pH approximately 5) the sixth coordination sites are filled by H(2)O that, o