Abstract
Ferredoxin, cytochrome c 3 and hydrogenase are specific partners of the sulfate reduction pathway of Desulfovibrio desulfuricans Norway and might be exemplary for electron exchange mechanism studies. Cytochrome c 3 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 c 3 should allow a discussion on the nature of the interaction. 1H-NMR spectra of ferredoxin I and cytochrome c 3 in the absence and presence of ferredoxin are presented.
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