Analyses of the electronic structures of FeFe-cofactors compared with those of FeMo- and FeV-cofactors and their P-clusters

• Published in: Dalton transactions : an international journal of inorganic chemistry Vol. 53; no. 15; pp. 6529 - 6536
• Main Authors: Xie, Zhen-Lang, Jin, Wan-Ting, Zhou, Zhao-Hui
• Format: Journal Article
• Language: English
• Published: England Royal Society of Chemistry 16.04.2024
• Subjects: Clusters; Crystallography; Iron; Mathematical analysis; Molybdenum; Oxidation; Proteins; Valence
• DOI: 10.1039/d3dt04126c
• ISSN: 1477-9226; 1477-9234

The electronic structures of FeFe-cofactors (FeFe-cos) in resting and turnover states, together with their P N clusters from iron-only nitrogenases, have been calculated using the bond valence method, and their crystallographic data were reported recently and deposited in the Protein Data Bank (PDB codes: 8BOQ and 8OIE ). The calculated results have also been compared with those of their homologous Mo- and V-nitrogenases. For FeFe-cos in the resting state, Fe1/2/4/5/6/7/8 atoms are prone to Fe 3+ , while the Fe3 atom shows different degrees of mixed valences. The results support that the Fe8 atom at the terminal positions of FeFe-cos possesses the same oxidation states as the Mo 3+ /V 3+ atoms of FeMo-/FeV-cos. In the turnover state, the overall oxidation state of FeFe-co is slightly reduced than those in the resting species, and its electronic configuration is rearranged after the substitution of S2B with OH, compatible with those found in CO-bound FeV-co. Moreover, the calculations give the formal oxidation states of 6Fe 2+ -2Fe 3+ for the electronic structures of P N clusters in Fe-nitrogenases. By the comparison of Mo-, V- and Fe-nitrogenases, the overall oxidation levels of 7Fe atoms (Fe1-Fe7) for both FeFe- and FeMo-cos in resting states are found to be higher than that of FeV-co. For the P N clusters in MoFe-, VFe- and FeFe-proteins, they all exhibit a strong reductive character. The electronic structures of FeFe-cofactors and their P N clusters from Fe-nitrogenases have been calculated using a BVS method from PDB protein structures and compared with those of Mo- and V-nitrogenases.