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Electron nuclear double resonance of the resting state of nitrogenase molybdenum iron proteins from azotobacter vinelandii klebsiella pneumoniae and clostridium pasteurianum hydrogen 1 iron 57 molybdenum 95 and sulfur 33 studies

Electron nuclear double resonance of the resting state of nitrogenase molybdenum iron proteins from azotobacter vinelandii klebsiella pneumoniae and clostridium pasteurianum hydrogen 1 iron 57 molybdenum 95 and sulfur 33 studies

Journal of the American Chemical Society 108(12): 3487-3498

Electron nuclear double resonance (ENDOR) studies of native and isotopically enriched MoFe proteins hold the promise of individually characterizing every atom of the catalytically active FeMo-co cluster of the nitrogenase MoFe protein. This report presents 1H, 57Fe, 95,97Mo, and 33S ENDOR measurements in a comparison of the MoFe protein isolated from the three titled organisms, Avl, Kpl, and Cpl. We have examined in detail single-crystal-like 57Fe resonances from at least five distinct iron sites in each of the three enzymes, revising somewhat our earlier assignments. The analysis incidentally gives the electron spin zero-field splitting parameters to high precision. 95Mo ENDOR measurements for Cpl and Kpl give 95Mo hyperfine and quadrupole coupling constants. They indicate that a single molybdenum is integrated into the MoFe spin system and that the molybdenum is most plausibly viewed as being in an even-electron state, which may be assigned provisionally as unsymmetrically coordinated MoIV. The observation of an exchangeable proton or protons from each protein source suggests a site on the cluster accessible to solvent and perhaps containing H2O or OH-. Cpl enriched in 33S gives the first observed ENDOR signals from this nucleus. The resonances from 33S are assignable to the inorganic sulfur because, it is argued, the FeMo-co cluster must be bound to the protein primarily, if not exclusively, by residues other than cysteinyl.

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