Advances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis

Robert Callender, R. Brian Dyer

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Time-resolved studies of enzymes date more than 100 years ago with the success of the Michaelis-Menton description of enzyme kinetics. For more than a century, approach development has been crucial toward the goal of a determination of the time evolution of atomic structure. To date, proven techniques to study enzymes include laser-induced temperature-jump (T-jump), time-resolved spectroscopic probes, laser-induced pH-Jump and rapid mixing methods. One way or another, these techniques have been applied to the study of triosephosphate isomerase (TIM), lactate dehydrogenase (LDH)-laser-induced T-Jump studies, hydride transfer in transhydrogenase and hydrolysis reaction of the Ras protein.

Original languageEnglish (US)
Pages (from-to)3031-3042
Number of pages12
JournalChemical Reviews
Volume106
Issue number8
DOIs
StatePublished - Aug 2006

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Catalysis
Lasers
Triose-Phosphate Isomerase
ras Proteins
Enzyme kinetics
Time and motion study
Enzymes
L-Lactate Dehydrogenase
Hydrides
Hydrolysis
Temperature

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Advances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis. / Callender, Robert; Dyer, R. Brian.

In: Chemical Reviews, Vol. 106, No. 8, 08.2006, p. 3031-3042.

Research output: Contribution to journalArticle

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