Bromination of Quorum Sensing Molecules: Vanadium Bromoperoxidase and Cerium Dioxide Nanocrystals via Free Active Bromine Transform Bacterial Communication.

The halogenation of quorum sensing molecules (QSMs) is known to be catalyzed by enzymes such as haloperoxidase (HPO) as well as cerium dioxide nanocrystals (NC), which mimic enzymes. Those enzymes and mimics can influence biological processes such as biofilm formation, where bacteria use QSMs for the "chemical" communication between each other and the coordination of surface colonization. However, not much is known about the degradation behavior of a broad spectrum of QSMs, especially for HPO and its mimics. Therefore, in this study, the degradation of three QSMs with different molecule moieties was elucidated. For this purpose, different batch experiments were carried out with HPOs, NCs and free active bromine (FAB). For N -β-ketocaproyl-homoserine lactone (3-Oxo-C 6 -AHL), N - cis -tetradec-9 Z -enoyl-homoserine lactone (C 14:1 -AHL) and 2-heptyl-4-quinolone (HHQ) a fast degradation and moiety-specific transformations were observed. The HPO vanadium bromoperoxidase as well as cerium dioxide NCs catalyzed the formation of the same brominated transformation products (TPs). Since the same TPs are formed in batch experiments with FAB it is very likely that FAB is playing a major role in the catalytical reaction mechanism leading to the transformation of QSMs. In this study in total 17 TPs could be identified in different levels of confidence and the catalytic degradation processes for two QS groups (unsaturated AHLs and alkyl quinolones) with cerium dioxide NCs and vanadium bromoperoxidase were expanded.