BORONIC ACIDS AS MECHANISTIC PROBES FOR THE BACTERIAL LUCIFERASE REACTION

Matthias Ahrens, Peter Macheroux, Anatol Eberhard, Sandro Ghisla, Bruce Branchaud, J. Woodland Hastings

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Abstract

Bacterial luciferase uses long chain aldehydes as substrates. Alkylboronic acid analogs of these substrates with chain lengths of C7 and C9 have been synthesized, characterized, and used as mechanistic probes for the light emitting reaction. They behave as inhibitors in the in vitro luminescence reaction. Contrary to an earlier report (Macheroux and Ghisla, 1985, Nachr. Chem. Tech. Lab. 33,785–790) they are not substrates for bacterial luciferase, in that they do not lead to light emission and are not oxidized by the flavin‐4a‐hydroperoxide to the products boric acid and the corresponding alcohol, as would be expected from a Baeyer‐Villiger reaction. However, the particular conformation of a putative boronic acid hydroperoxide at the active center might be such that it would preclude a Baeyer‐Villiger fragmentation. Thus, while the results do not support the postulate that luciferase proceeds via a Baeyer‐Villiger mechanism, they also do not exclude it. A further observation was that the endogenous light emission (no added aldehyde) decays more rapidly than does the luciferase bound flavin‐4a‐hydroperoxide. This suggests that the endogenous light is not caused by the decomposition of the flavin‐4a‐hydroperoxide.

Original languageEnglish (US)
Pages (from-to)295-299
Number of pages5
JournalPhotochemistry and Photobiology
Volume54
Issue number2
DOIs
Publication statusPublished - Jan 1 1991
Externally publishedYes

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ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry
  • Physical and Theoretical Chemistry

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