Do vesicle cells of the red alga Asparagopsis (Falkenbergia stage) play a role in bromocarbon production?

The Rhodophyceae (red algae) are an established source of volatile halocarbons in the marine environment. Some species in the Bonnemaisoniaceae have been reported to contain large amounts of halogens in structures referred to as vesicle cells, suggesting involvement of these specialised cells in the production of halocarbons. We have investigated the role of vesicle cells in the accumulation and metabolism of bromide in an isolate of the red macroalga Asparagopsis (Falkenbergia stage), a species known to release bromocarbons. Studies of laboratory-cultivated alga, using light microscopy, revealed a requirement of bromide for both the maintenance and formation of vesicle cells. Incubation of the alga in culture media with bromide concentrations below 64 mg l-1 (the concentration of Br- in seawater) resulted in a decrease in the proportion of vesicle cells to pericentral cells. The abundance of vesicle cells was correlated with bromide concentration below this level. Induction of vesicle cell formation in cultures of Falkenbergia occurred at concentrations as low as 8 mg l-1, with the abundance of vesicle cells increasing with bromide concentration up to around 100 mg l-1. Further studies revealed a positive correlation between the abundance of vesicle cells and dibromomethane and bromoform production. Interestingly, however, whilst dibromomethane production was stimulated by the presence of bromide in the culture media, bromoform release remained unaffected suggesting that the two compounds are formed by different mechanisms.

Enantiocomplementary preparation of (S)- and (R)-1-pyridylalkanols via ketone reduction and alkane hydroxylation using whole cells of Pseudomonas putida UV4

A previously unreported alcohol dehydrogenase enzyme in the mutant soil bacterium Pseudomonas putida UV4 catalyses the reduction of 2-, 3- and 4-acylpyridines to afford the corresponding (S)-1-pyridyl alkanols, with moderate to high e.e., whilst under the same conditions 2,6-diacetylpyridine is readily converted to the corresponding enantiopure C2-symmetric (S,S)-diol in one step. In contrast, the toluene dioxygenase enzyme in the same organism catalyses the hydroxylation of 2- and 3-alkylpyridines to (R)-1-(2-pyridyl) and (R)-1-(3-pyridyl)alkanols. This combination of oxidative and reductive biotransformations thus provides a method for preparing both enantiomers of chiral 1-pyridyl alkanols using one biocatalyst.