Abstract
Electron spin echo envelope modulation (ESEEM) spectroscopy, a pulsed electron spin resonance technique, was used to analyze the N coordination of the iron-molybdenum (FeMo) cofactor contained within the nitrogenase MoFe protein. Comparison of spectra obtained from whole cells and purified MoFe protein established that the N coordination of the FeMo cofactor provided by the MoFe-protein polypeptide matrix can be unambiguously recognized in whole cells. ESEEM spectra of altered MoFe proteins, which were produced in certain mutant strains of Azotobacter vinelandii, showed that the N coordination to FeMo cofactor requires His-195 of the MoFe protein alpha subunit. Moreover, this requirement for His-195 was shown to be essential for biological nitrogen fixation.
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