Perspectives on the mechanism of ATP hydrolysis by nitrogenase

Stephan O. Krause, William G. Gutheil, Anton M. Simeonov, Terry O. Matsunaga, Margaret J. Stauber, George L. Kenyon, Charles E. Mckenna

Research output: Contribution to journalReview article

Abstract

The chemical mechanism of ATP hydrolysis by nitrogenase is discussed in terms of results from isotopic exchange studies using [18O4]-Pi, b,g-[18O]-ATP, and g-[18O4]-ATP as probes of reversibility (ATP = ADP + Pi) and of the freedom of rotation around the O-Pb bond in enzyme-bound ADP.

Original languageEnglish (US)
Pages (from-to)513-516
Number of pages4
JournalPhosphorus, Sulfur and Silicon and Related Elements
Volume144-146
DOIs
StatePublished - Jan 1 1999
Externally publishedYes

    Fingerprint

Keywords

  • ATP hydrolysis
  • HRMS
  • Nitrogenase
  • P NMR
  • PIX
  • [O]-phosphate
  • g-[O]-ATP

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Inorganic Chemistry

Cite this

Krause, S. O., Gutheil, W. G., Simeonov, A. M., Matsunaga, T. O., Stauber, M. J., Kenyon, G. L., & Mckenna, C. E. (1999). Perspectives on the mechanism of ATP hydrolysis by nitrogenase. Phosphorus, Sulfur and Silicon and Related Elements, 144-146, 513-516. https://doi.org/10.1080/10426509908546294