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Previous Mössbauer and EPR studies of the MoFe protein (approximately 30 Fe and 2 Mo) of nitrogenase have revealed the presence of two unique clusters, namely, the P-clusters (presumably of the Fe4S4 type) and the molybdenum- and iron-containing cofactors (or M-clusters). Mössbauer components D (approximately 10-12 Fe) and Fe2+ (approximately 4 Fe) represent subsites of the P-clusters while component S (approximately 2 Fe) appeared to belong to a separate, unidentified cluster. In order to refine the analyses of Mössbauer spectra, we have constructed an isotopic hybrid of the Klebsiella pneumoniae protein which contains 57Fe-enriched P-clusters and 56Fe-enriched M-clusters. The highly resolved 57Fe Mössbauer spectra of this hybrid show that component S behaves spectroscopically like the P-cluster sites D and Fe2+ in oxidized and reduced MoFe protein. This suggests that S is a subset of the P-clusters rather than a different cluster type. The present study shows, for the first time, that the Debye-Waller factors of different P-cluster subsites have a different temperature dependence. Thus, the Fe2+/D absorption ratio is 4.0:10.0 at 4.2 K and 4.0:11.6 at 173 K. We propose that the reduced MoFe protein contains two pairs of P-clusters: one pair containing one Fe2+ and three D-sites and the other one Fe2+, two D, and one S-site. We have argued previously that the oxidized P-clusters occur in pairs as well.
McLean et al. (Tue,) studied this question.