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 language | English (US) |
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Pages (from-to) | 513-516 |
Number of pages | 4 |
Journal | Phosphorus, Sulfur and Silicon and Related Elements |
Volume | 144-146 |
DOIs | |
State | Published - 1999 |
Externally published | Yes |
Keywords
- ATP hydrolysis
- HRMS
- Nitrogenase
- P NMR
- PIX
- [O]-phosphate
- g-[O]-ATP
ASJC Scopus subject areas
- Biochemistry
- Organic Chemistry
- Inorganic Chemistry