The distribution of dimethylsulphide (DMS), together with the precursor dimethylsulphonio-propionate (DMSP) and the oxidation product dimethylsulphoxide (DMSO), was measured in melt waters on the McMurdo Ice Shelf in the immediate vicinity of Bratina Island. Conductivity in these sulphate dominated ponds was extremely variable, ranging from 0.106–52.3 mS cm−1. Similarly, chlorophyll a concentrations in the pond waters (1–150 μg 1−1) and mats (1.4–33 μg cm−2) differed considerably. The biomass was dominated by benthic felts of phototrophic cyanobacteria, which might act as a source of biogenic sulphur compounds in the ponds. The mean (and ranges) of concentrations of dissolved sulphur compounds (nmol 1−1) were: CS2 0.16 (<0.04–1.29); DMSPd 0.6 (<0.07–8.4); DMS 3.5 (<0.07–183); DMSO 27.9 (15.5–184.5). Very high concentrations of DMSO were ubiquitous in the ponds in the ice-cored moraine region of the ice shelf, with dissolved concentrations having been 1–2 orders of magnitude greater than those of DMS or DMSPd. It is difficult to ascribe the formation of DMSO solely to the conventionally accepted pathways of DMS oxidation by either bacterial activity or photochemical reactions. A direct biosynthetic production from phytoplankton or bacteria might be involved which means that DMSO in aquatic environments could act as a significant source of DMS rather than as a sink as generally supposed.

The universally conserved A2451 of 23S rRNA has been proposed to participate directly in the catalysis of peptide bond formation in the ribosomal peptidyl transferase center. An unusually high, near neutral, pKa of A2451 is a prerequisite for its action as a general acid–base catalyst. Increased reactivity of A2451 to dimethylsulfate (DMS) at pH 8.5 compared to pH 6.5 was taken as evidence that the pKa of this nucleotide falls within this pH range. Structural data suggested that the interaction between A2451 and G2447 in the ribosome is responsible for A2451 pKa perturbation. In contrast to expectation, our studies did not show pH dependence of A2451 dimethylsulfate modification in ribosomes of Thermus aquaticus and Mycobacterium smegmatis. Other rRNA regions, however, showed major alterations in DMS reactivity at pH 8.5 compared to pH 6.5, suggesting that conformational rearrangements in the structure of the large ribosomal subunit may occur upon the pH shift. The G2447U mutant of M. smegmatis was viable, indicating that the G2447-A2451 interaction is not critical for the ribosome function. We concluded that the proposed unusual pKa of A2451, if existing, may not be crucial for the ribosome activity and that the previously reported pH-dependent alterations in the DMS modification of A2451 do not necessarily reveal an unusual pKa of this nucleotide.