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The reaction of cytochrome c with trifluoromethylphenyl isocyanate was carried out under conditions which led to the modification of a small number of the 19 lysines. Extensive ion-exchange chromatography was used to separate and purify six different derivatives, each modified at a single lysine residue, lysines 8, 13, 27, 72, 79, and 100, respectively. The only modifications which affected the activity of cytochrome c with cytochrome oxidase (EC 1.9.3.1) were those of lysines immediately surrounding the heme crevice, lysines 13, 27, 72, and 79, and also lysine 8 at the top of the heme crevice. In each case, the modified cytochrome c had the same maximum velocity as that of native cytochrome c, but an increased Michaelis constant for high affinity phase of the reaction. This supports the hypothesis that the cytochrome oxidase reaction site is located in the heme crevice region, and the highly conserved lysine residues surrounding the heme crevice are important in the binding.
H T Smith, and
N Staudenmayer, and
F Millett
December 1980,
Biochimica et biophysica acta,
H T Smith, and
N Staudenmayer, and
F Millett
February 1981,
The Journal of biological chemistry,
H T Smith, and
N Staudenmayer, and
F Millett
July 1992,
Biochemistry and cell biology = Biochimie et biologie cellulaire,
H T Smith, and
N Staudenmayer, and
F Millett
January 1982,
Biochimica et biophysica acta,
H T Smith, and
N Staudenmayer, and
F Millett
September 1978,
The Journal of biological chemistry,
H T Smith, and
N Staudenmayer, and
F Millett
February 1965,
The Journal of biological chemistry,
H T Smith, and
N Staudenmayer, and
F Millett
January 1973,
The Journal of biological chemistry,
H T Smith, and
N Staudenmayer, and
F Millett
February 1979,
Biochemical and biophysical research communications,
H T Smith, and
N Staudenmayer, and
F Millett
August 1977,
Biochimica et biophysica acta,
H T Smith, and
N Staudenmayer, and
F Millett
September 1980,
Biochemistry,
