PMID: 11607203Aug 1, 1991Paper

N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation

Proceedings of the National Academy of Sciences of the United States of America
H ThomannD R Dean

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.

Citations

Jun 6, 2009·Annual Review of Biochemistry·Lance C SeefeldtDennis R Dean
Aug 19, 2016·Dalton Transactions : an International Journal of Inorganic Chemistry·Ian Dance
Mar 12, 2010·Dalton Transactions : an International Journal of Inorganic Chemistry·Yilin HuMarkus W Ribbe
Dec 6, 2019·Chembiochem : a European Journal of Chemical Biology·Ian Dance
Jan 29, 2014·Chemical Reviews·Brian M HoffmanLance C Seefeldt
May 8, 2003·Journal of the American Chemical Society·Hong-In LeeBrian M Hoffman
Nov 7, 1996·Chemical Reviews·Barbara K. Burgess, David J. Lowe

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