Sequence-specific C-13 and N-15 NMR assignments for the oxidized form of the 2[Fe4S4](2+) ferredoxin from Clostridium pasteurianum are presented. Partial or complete sequence-specific H-1 NMR assignments for 52 of the 55 amino acid residues are also derived, extending those previously identified in this paramagnetic protein (Gaillard J.; Moulis, J.-M.; Kummerle, R.; Meyer, J. Magn. Reson. Chem. 1993, 31, 527). Protons which remain unassigned are in regions close to the paramagnetic clusters. The H-1 resonances for all but nine non-cysteinyl amide groups have been assigned specifically. Those which have not been assigned are all likely NH ... S donors to either a cluster sulfide or cysteinyl S-gamma. Eight of the nine are symmetry-related (V9/I38, G12/G41, A13/N42 and A22/A51). Eight paramagnetically shifted non-proline N-15 resonances (140-170 ppm) exhibit a pairwise arrangement in two-dimensional N-15 acquired INEPT experiments. The NH functions of symmetry-related residues Cys 47 and Cys 18 have been assigned specifically. Assignments for the NH functions for symmetry-related residues Cys 14 and Cys 43 are made on the basis of their close proximity to the paramagnetic centers.