The oxidized 7Fe-8S ferredoxin from
Rhodopseudomonas palustris is shown to possessaunique
1H NMR spectrum displaying at least onehyperfine-shifted
-CH
2 signal for each cysteineboundto the [3Fe-4S] cluster. COSY and TOCSY spectra and 1- and2-dimensional NOE experiments, inconjunction with a thorough reexamination of the
1H NMRdata on similar systems, permitted the sequentialassignment of all of the cysteine
-CH
2 protons even inthe absence of the amino acid sequence. Thesequential assignment stems on the homology of the hyperfine shiftpattern with those of other sequenced7Fe-8S ferredoxins, which points to a substantial homology in tertiarystructure. From the assignment,an analysis of the antiferromagnetic coupling in the [3Fe-4S] systemwas performed on the basis of ageneral model of exchange coupling. The NMR signal patterns of[3Fe-4S] clusters in both 3Fe-4S and7Fe-8S ferredoxins have been discussed, and some correlations areproposed between signal patterns andthe primary sequence.