Assignment of the cysteinyl 13C nuclear magnetic resonances and comparison of other aliphatic amino acid resonances of Clostridium acidi-urici, Clostridium pasteurianum, and Peptococcus aerogenes ferredoxins.
13C NMR spectra of Clostridium acidi-urici, Clostridium pasteurianum, and Peptococcus aerogenes ferredoxins show that some 13C resonances of the aliphatic amino acid residues are shifted significantly from their corresponding resonance positions in the spectra of model polypeptides or apoferredoxin. Thirteen 13C resonances are shifted into the 80- to 120-ppm (from CS2) region, and have been assigned to the cysteinyl alpha and beta carbon atoms. The remaining shifted resonances in the 120- to 190-ppm region are tentatively assigned to amino acid residues that may be close to [4Fe-4S] clusters of the oxidized and reduced ferredoxins. The similarity in the shift pattern of the corresponding 13C resonances of the cysteinyl alpha and beta carbon atoms in the three ferredoxins studied suggests that the three-dimensional amino acid environments of the corresponding [4Fe-4S] clusters in each protein are similar.
D000596:Amino Acids / Q000032:analysis*; D003013:Clostridium / Q000032:analysis*; D003545:Cysteine / Q000032:analysis*; D005288:Ferredoxins / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D010460:Peptococcus / Q000032:analysis*; D011487:Protein Conformation; D013045:Species Specificity
D000596:Amino Acids; D005288:Ferredoxins; D003545:Cysteine