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BORONIC ACIDS AS MECHANISTIC PROBES FOR THE BACTERIAL LUCIFERASE REACTION
Author(s) -
Ahrens Matthias,
Macheroux Peter,
Eberhard Anatol,
Ghisla Sandro,
Branchaud Bruce P.,
Hastings J. Woodland
Publication year - 1991
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1991.tb02019.x
Subject(s) - luciferase , flavin group , chemistry , light emission , boronic acid , aldehyde , chemiluminescence , stereochemistry , photochemistry , combinatorial chemistry , biochemistry , enzyme , organic chemistry , catalysis , physics , optoelectronics , gene , transfection
References Bacterial luciferase uses long chain aldehydes as substrates. Alkylboronic acid analogs of these substrates with chain lengths of C 7 and C 9 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.