Statistical analyses of the oxidized P‐clusters in MoFe proteins using the bond‐valence method: towards their electron transfer in nitrogenases.

26 well selected oxidized P‐clusters (P2+) from the crystallographic data deposited in the Protein Data Bank have been analysed statistically by the bond‐valence sum method with weighting schemes for MoFe proteins at different resolutions. Interestingly, the oxidation states of P2+ clusters correspond to Fe23+Fe62+ with high electron delocalization, showing the same oxidation states as the resting states of P‐clusters (PN) in nitrogenases. The previously uncertain reduction of P2+ to PN clusters by two electrons was assigned as a double protonation of P2+, in which decoordination of the serine residue and the peptide chain of cysteine take place, in MoFe proteins. This is further supported by the obviously shorter α‐alkoxy C—O bond (average of 1.398 Å) in P2+ clusters and longer α‐hydroxy C—O bond (average of 1.422 Å) in PN clusters, while no change is observed in the electronic structures of Fe8S7 Fe atoms in P‐clusters. Spatially, the calculations show that Fe3 and Fe6, the most oxidized and most reduced Fe atoms, have the shortest distances of 9.329 Å from the homocitrate in the FeMo cofactor and 14.947 Å from the [Fe4S4] cluster, respectively, and may well function as important electron‐transport sites. [ABSTRACT FROM AUTHOR]