Electron transfer between horse ferritin and ferrihaemoproteins.
Reactions of reduced horse spleen ferritin with horse and Saccharomyces cerevisiae ferricytochromes c, cow ferricytochrome b5, sperm-whale metmyoglobin and Pseudomonas aeruginosa ferricytochrome c-551 were investigated by u.v.-visible spectrophotometry. In all cases the reduced ferritin reduced the ferrihaemoproteins. The rate of reduction varied from less than 0.2 M-1.s-1 for metmyoglobin to 1.1 x 10(3) M-1.s-1 for horse ferricytochrome c (0.1 M-phosphate buffer, pH 7.4, at 25 degrees C). We conclude that the mechanism of ferrihaemoprotein reduction involves long-range electron transfer through the coat of ferritin and that such electron transfer is rapid enough to account for the rates of iron release observed by other workers in reductive release assays.
Kadir
F H
FH
Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, U.K.
al-Massad
F K
FK
Fatemi
S J
SJ
Singh
H K
HK
Wilson
M T
MT
Moore
G R
GR
D000818:Animals; D001426:Bacterial Proteins; D003574:Cytochrome c Group / Q000378:metabolism; D003580:Cytochromes / Q000378:metabolism*; D015786:Cytochromes b5 / Q000378:metabolism; D004579:Electron Transport; D005293:Ferritins / Q000378:metabolism*; D006736:Horses; D009211:Myoglobin / Q000378:metabolism; D010084:Oxidation-Reduction; D013056:Spectrophotometry, Ultraviolet
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D003580:Cytochromes; D009211:Myoglobin; D005293:Ferritins; D015786:Cytochromes b5; C017167:cytochrome C(551)