Mapping Enzyme Landscapes by Time-Resolved Crystallography with Synchrotron and X-Ray Free Electron Laser Light

Mark A. Wilson

Research output: Contribution to journalReview articlepeer-review

2 Scopus citations

Abstract

Directly observing enzyme catalysis in real time at the molecular level has been a long-standing goal of structural enzymology. Time-resolved serial crystallography methods at synchrotron and X-ray free electron laser (XFEL) sources have enabled researchers to follow enzyme catalysis and other nonequilibrium events at ambient conditions with unprecedented time resolution. X-ray crystallography provides detailed information about conformational heterogeneity and protein dynamics, which is enhanced when time-resolved approaches are used. This review outlines the ways in which information about the underlying energy landscape of a protein can be extracted from X-ray crystallographic data, with an emphasis on new developments in XFEL and synchrotron time-resolved crystallography. The emerging view of enzyme catalysis afforded by these techniques can be interpreted as enzymes moving on a time-dependent energy landscape. Some consequences of this view are discussed, including the proposal that irreversible enzymes or enzymes that use covalent catalytic mechanisms may commonly exhibit catalysis-activated motions.

Original languageEnglish (US)
Pages (from-to)79-98
Number of pages20
JournalAnnual Review of Biophysics
Volume51
DOIs
StatePublished - 2022

Keywords

  • X-ray free electron laser
  • XFEL
  • conformational ensembles
  • fluctuation-dissipation relation
  • nonequilibrium protein dynamics
  • time-resolved crystallography

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Bioengineering
  • Biochemistry
  • Cell Biology

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