Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids.
The alkaline transitions of tuna and horse ferricytochromes c and the trifluoroacetyl-lysine derivative of horse ferricytochrome c have been studied by Fourier-transform (FT) i.r. spectroscopy. The spectral perturbations resulting from the transition have been interpreted by reference to FT i.r. data on simple carboxylic-acid-containing compounds and a bacterial cytochrome c551 in which a haem propionate ionizes without causing a significant conformational change. The analysis strongly suggests that ionization of a haem propionate of mitochondrial cytochrome c triggers the alkaline conformation change.
Tonge
P
P
Department of Biochemistry, University of Birmingham, U.K.
Moore
G R
GR
Wharton
C W
CW
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D002264:Carboxylic Acids / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D005583:Fourier Analysis; D006418:Heme / Q000378:metabolism; D006736:Horses; D006863:Hydrogen-Ion Concentration; D008928:Mitochondria / Q000378:metabolism*; D011422:Propionates / Q000378:metabolism; D011550:Pseudomonas aeruginosa; D013055:Spectrophotometry, Infrared
D001426:Bacterial Proteins; D002264:Carboxylic Acids; D003574:Cytochrome c Group; D011422:Propionates; D006418:Heme; C029658:propionic acid