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pro vyhledávání: '"Michael T. Wilson"'
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:
The Biochemical journal. 434(3)
Cytoglobin is a recently discovered hexa-co-ordinate haemoglobin that does not appear to function as a classical oxygen-binding protein. Its function is unknown and studies on the effects of changes in its expression have not decisively determined it
Autor:
Colin Greenwood, Michael T. Wilson
Publikováno v:
European Journal of Biochemistry. 22:11-18
1 A model is proposed to explain the biphasic reduction of ferricytochrome c at alkaline pH assuming an equilibrium distribution between a reducible and non-reducible conformer. An analysis of this model is given in an appendix to this paper. 2 Prote
Studies on partially reduced mammalian cytochrome oxidase: reactions with carbon monoxide and oxygen
Publikováno v:
Scopus-Elsevier
A number of methods were used to prepare a species of mammalian cytochrome oxidase (EC 1.9.3.1, ferrocytochrome c –oxygen oxidoreductase) in which only cytochrome a 3 is reduced and in combination with CO. The kinetics of CO binding by cytochrome a
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