Structural dynamics in F1ATPase during the first reaction cycle of ATP hydrolysis

FEBS Letters

Dose, Klaus²  Hütsch, Matthias¹  Nawroth, Thomas²  Neidhurdt, Axel² 

[1] DESY/HASYLAB, D-2000 Hamburg 52, Germany;Institut für Biochemie, Johannes Gutenberg-Universität Mainz, D-6500 Mainz, Germany

关键词: F1ATPase;    Reaction cycle;    Dynamic structure transition;    Time resolved X-ray scattering;   

DOI  :  10.1016/0014-5793(91)80232-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The velocity of ATP hydrolysis, catalyzed by purified F₁ATPase from Micrococcus luteus, was decelerated on decreasing the temperature. At 13′C one reaction cycle is completed after 20 s. Hydrolysis was triggered upon rapid mixing of the enzyme with ATP. During the first reaction cycle, succeeding structural alterations of the F₁ATPase were traced by time resolved X-ray scattering. The scattering spectra obtained from consecutive intervals of 1 s, revealed the F₁ATPase to pass a conformational state exhibiting an expanded (6%) molecular shape. The expanded state was observed between 45% and 65% of the time required to complete the reaction cycle. This pointx out a conformational pulsation during ATP hydrolysis.

【 授权许可】

Unknown