Electron transfer mechanism and interaction studies between cytochrome C3 and ferredoxin.
Ferredoxin, cytochrome c3 and hydrogenase are specific partners of the sulfate reduction pathway of Desulfovibrio desulfuricans Norway and might be exemplary for electron exchange mechanism studies. Cytochrome c3 contains four low redox potential haems for 13 000 molecular weight. Two ferredoxins isolated from the same bacteria are dimers of 6 000 molecular weight per subunit (Ferredoxin I: one (4 Fe-4S) cluster per subunit, ferredoxin II: two (4 Fe-4 S) clusters per subunit). The amino acid sequence of ferredoxin I is reported and compared to the ferredoxin II sequence. The structural characteristics of ferredoxins and cytochrome c3 should allow a discussion on the nature of the interaction. 1H-NMR spectra of ferredoxin I and cytochrome c3 in the absence and presence of ferredoxin are presented.
D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000302:isolation & purification / Q000378:metabolism*; D003901:Desulfovibrio / Q000378:metabolism*; D004579:Electron Transport; D005288:Ferredoxins / Q000302:isolation & purification / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011485:Protein Binding; D013045:Species Specificity
D003574:Cytochrome c Group; D005288:Ferredoxins; C017165:cytochrome c(3)