Competitive 15M kinetic isotope effects of nitrogenase-catalyzed dinitrogen reduction

Amandeep K. Sra, Yilin Hu, Glen E. Martin, Daniel D. Snow, Markus W. Ribbe, Amnon Kohen

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Biological N2 fixation is achieved under ambient conditions by enzymatic catalysis. The enzyme nitrogenase has been studied extensively, but the N2 chemical reduction step is, by far, not rate limiting and hard to examine. A new method was developed that allows studying the reduction transition state within the enzyme's complex kinetic cascade by means of the 15N kinetic isotope effect on the reaction's second-order rate constant, V/K. A value of 1.7% ± 0.2% was measured.

Original languageEnglish (US)
Pages (from-to)12768-12769
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number40
StatePublished - Oct 13 2004

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Sra, A. K., Hu, Y., Martin, G. E., Snow, D. D., Ribbe, M. W., & Kohen, A. (2004). Competitive 15M kinetic isotope effects of nitrogenase-catalyzed dinitrogen reduction. Journal of the American Chemical Society, 126(40), 12768-12769.