N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.
Year: 1991
Type: article
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.
Authors: H Thomann, M Bernardo, W E Newton, D R Dean
Institution: ExxonMobil (United States)
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W1997426478