Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer

W. J. Bruno, W. Bialek

Research output: Contribution to journalArticle

124 Scopus citations

Abstract

We present a theory of enzymatic hydrogen transfer in which hydrogen tunneling is mediated by thermal fluctuations of the enzyme's active site. These fluctuations greatly increase the tunneling rate by shortening the distance the hydrogen must tunnel. The average tunneling distance is shown to decrease when heavier isotopes are substituted for the hydrogen or when the temperature is increased, leading to kinetic isotope effects (KIEs)--defined as the factor by which the reaction slows down when isotopically substituted substrates are used--that need be no larger than KIEs for nontunneling mechanisms. Within this theory we derive a simple KIE expression for vibrationally enhanced ground state tunneling that is able to fit the data for the bovine serum amine oxidase (BSAO) system, correctly predicting the large temperature dependence of the KIEs. Because the KIEs in this theory can resemble those for nontunneling dynamics, distinguishing the two possibilities requires careful measurements over a range of temperatures, as has been done for BSAO.

Original languageEnglish (US)
Pages (from-to)689-699
Number of pages11
JournalBiophysical Journal
Volume63
Issue number3
DOIs
StatePublished - 1992
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics

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