6533b82ffe1ef96bd1295c8e
RESEARCH PRODUCT
Structural dynamics in F1ATPase during the first reaction cycle of ATP hydrolysis
Klaus DoseMatthias HütschThomas NawrothAxel Neidhurdtsubject
Reaction mechanismProtein ConformationStereochemistryATPaseBiophysicsTime resolved X-ray scatteringBiochemistryMicrococcusCatalysisF1ATPaseHydrolysisMolecular dynamicsAdenosine TriphosphateStructural BiologyATP hydrolysisGeneticsMolecular Biologychemistry.chemical_classificationbiologyHydrolysisX-RaysReaction cycleCell Biologybiology.organism_classificationKineticsProton-Translocating ATPasesEnzymechemistryDynamic structure transitionbiology.proteinMicrococcus luteusdescription
Abstract The velocity of ATP hydrolysis, catalyzed by purified F 1 ATPase 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 F 1 ATPase were traced by time resolved X-ray scattering. The scattering spectra obtained from consecutive intervals of 1 s, revealed the F 1 ATPase 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1991-03-11 | FEBS Letters |