Dimethylsulphoniopropionate (DMSP) is one of the Earth’s most abundant organosulphur molecules, a signalling molecule, a key nutrient for marine microorganisms, and the major precursor for gaseous dimethyl sulphide (DMS). DMS, another infochemical in signalling pathways, is important in global sulphur cycling2, and affects the Earth’s albedo, and potentially climate, via sulphate aerosol and cloud condensation nuclei production. It was thought that only eukaryotes produce significant amounts of DMSP, but here we demonstrate that many marine heterotrophic bacteria also produce DMSP, likely using the same methionine (Met) transamination pathway as macroalgae and phytoplankton10. We identify the first DMSP synthesis gene in any organism, dsyB, which encodes the key methyltransferase enzyme of this pathway and is a reliable reporter for bacterial DMSP synthesis in marine alphaproteobacteria. DMSP production and dsyB transcription are upregulated by increased salinity, nitrogen limitation and lower temperatures in our model DMSP-producing bacterium Labrenzia aggregata LZB033. With significant numbers of dsyB homologues in marine metagenomes, we propose that bacteria likely make a significant contribution to oceanic DMSP production. Furthermore, since DMSP production is not solely associated with obligate phototrophs, the process need not be confined to the photic zones of marine environments, and as such may have been underestimate

A bacterium in the genus Halomonas that grew on dimethylsulfoniopropionate (DMSP) or acrylate as sole carbon sources and that liberated the climate-changing gas dimethyl sulfide in media containing DMSP was obtained from the phylloplane of the macroalga Ulva. We identified a cluster that contains genes specifically involved in DMSP catabolism (dddD, dddT) or in degrading acrylate (acuN, acuK) or that are required to break down both substrates (dddC, dddA). Using NMR and HPLC analyses to trace 13C- or 14C-labelled acrylate and DMSP in strains of Escherichia coli with various combinations of cloned ddd and/or acu genes, we deduced that DMSP is imported by the BCCT-type transporter DddT, then converted by DddD to 3-OH-propionate (3HP), liberating dimethyl sulfide in the process. As DddD is a predicted acyl CoA transferase, there may be an earlier, unidentified catabolite of DMSP. Acrylate is also converted to 3HP, via a CoA transferase (AcuN) and a hydratase (AcuK). The 3HP is predicted to be catabolized by an alcohol dehydrogenase, DddA, to malonate semialdehyde, thence by an aldehyde dehydrogenase, DddC, to acyl CoA plus CO2. The regulation of the ddd and acu genes is unusual, as a catabolite, 3HP, was a co-inducer of their transcription. This first description of genes involved in acrylate catabolism in any organism shows that the relationship between the catabolic pathways of acrylate and DMSP differs from that which had been suggested in other bacteria.

The preparation of a series of diastereoisomeric tetracamphorsulfonates derived from racemic tetramethoxyresorcin [4]arenes was achieved by reactions with an excess of (S)-(+)-10-camphorsulfonyl chloride in pyridine followed by isolation using flash chromatography. Tetradeprotonation of a number of tetramethoxyresorcin[4]arenes using n-butyllithium in tetrahydrofuran, followed by reactions using (S)-(+)-10-camphorsulfonyl chloride, gave the same tetracamphorsulfonates. Mono-, di-and tricamphorsulfonates were also prepared following selective deprotonation. In the reactions with tetraisopropyloxy-and tetracyclopentyloxyresorcin[4]arenes, only the mono-and dicamphorsulfonates were formed. X-ray crystallographic analysis established the absolute configurations of three diastereoisomerically pure tetracamphorsulfonates, including a diastereoisomer preparedThe chemistry of calixarenes is widely studied and has provided a diverse range of molecular assemblies that have been used for a variety of purposes; the topic continues to generate considerable interest.[1] The acid-catalysed interaction of aldehydes with resorcinol provides a high-yield route to a range of cyclic tetramers that has made the study of resorcin [4]arenes, for example 1, particularly attractive. [2] The dissymmetry generated by the unsymmetrical substitution of calixarenes is recognized as being related to the nonplanar structures of the parent compounds, [3a] although a number of chiral calixarene conformers are racemized thermally by processes involving "through-the-annulus rota- [a]

Dynamics of a nonplanar GFP chromophore are studied experimentally and theoretically. Coupled torsional motion is responsible for the ultrafast decay.

An organocatalytic asymmetric epoxidation reaction using iminium salt catalysts is described, in which the stoichiometric persulfate oxidant is generated electrochemically. This system offers comparable ees to the use of commercially available persulfate. Electrochemically generated percarbonate ion is also a successful and novel oxidant system for use with iminium salts

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Kaede, an analogue of green fluorescent protein (GFP), is a green-to-red photoconvertible fluorescent protein used as an in vivo “optical highlighter” in bioimaging. The fluorescence quantum yield of the red Kaede protein is lower than that of GFP, suggesting that increasing the conjugation modifies the electronic relaxation pathway. Using a combination of anion photoelectron spectroscopy and electronic structure calculations, we find that the isolated red Kaede protein chromophore in the gas phase is deprotonated at the imidazole ring, unlike the GFP chromophore that is deprotonated at the phenol ring. We find evidence of an efficient electronic relaxation pathway from higher-lying electronically excited states to the S1 state of the red Kaede chromophore that is not accessible in the GFP chromophore. Rapid autodetachment from high-lying vibrational states of S1 is found to compete efficiently with internal conversion to the ground electronic state.

The photophysics of the chromophore of the green fluorescent protein in Aequorea victoria (avGFP) are dominated by an excited state proton transfer reaction. In contrast the photophysics of the same chromophore in solution are dominated by radiationless decay, and photoacid behaviour is not observed. Here we show that modification of the pKa of the chromophore by fluorination leads to an excited state proton transfer on an extremely fast (50 fs) time scale. Such a fast rate suggests a barrierless proton transfer and the existence of a pre-formed acceptor site in the aqueous solution, which is supported by solvent and deuterium isotope effects. In addition, at lower pH, photochemical formation of the elusive zwitterion of the GFP chromophore is observed by means of an equally fast excited state proton transfer from the cation. The significance of these results for understanding and modifying the properties of fluorescent proteins are discussed