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Area of Science:

  • Chemical kinetics
  • Biochemical reaction networks
  • Enzymatic catalysis

Background:

  • Chemical and biological transformations often occur via competing reaction pathways.
  • Enzymatic processes utilize biological catalysts to create novel reaction routes.
  • Current understanding assumes product formation is dictated by the fastest kinetic pathway.

Purpose of the Study:

  • To theoretically investigate the dominant factor in product formation at short time scales.
  • To challenge the prevailing assumption that fastest kinetics always govern reaction pathways.
  • To analyze the role of pathway length versus kinetic speed in chemical and biological systems.

Main Methods:

  • Theoretical analysis of competing reaction pathways.
  • Explicit calculation for a system with two competing reversible/irreversible pathways.
  • Examination of reaction dynamics at different time scales.

Main Results:

  • At sufficiently short time scales, reactions are predominantly determined by the shortest pathway (fewest intermediate states).
  • This effect occurs regardless of the average turnover time of the pathways.
  • A universal phenomenon is demonstrated for competing reaction systems.

Conclusions:

  • Pathway length, not just kinetic speed, is critical for understanding early-stage reactions.
  • The findings are relevant for interpreting single-molecule experimental data.
  • This work provides a new perspective on reaction network dynamics.