No abstract

The o and l isomers of some protein amino acids present In soils were measured by using a gas chromatographic technique. The results of two processing procedures were compared to determine the better method. Results of the comparison indicated that the determination of o and l percentages requires amino acid purification If one is tb obtain accurate data. It was found that very significant amounts of o-alartlne, o-aspartic acid, and o-glutamic acid were present in the contemporary soils studied. Valine, isoleucine, leucine, proline, and phenylalanine generally contained only, a trace to very Small amounts of the o isomer. It is probable that the o-amlno acids from the alanine, aspartic, and glutamic acids are contributed to the soil primarily via microorganisms. The flridlng of very significant quantities of some D-amino acids (~S-16%)In present-day soils may alert some Investigators of geological sediments to a possible problem In using amino acid racemization as an age-dating technique.

Lipophilic pigments were examined in microbial mat communities dominated by cyanobacteria in the intertidal zone and by diatoms in the subtidal and sublittoral zones of Hamelin Pool, Shark Bay, Western Australia. These microbial mats have evolutionary significance because of their similarity to lithfied stromatolites from the Proterozoic and Early Paleozoic eras. Fucoxanthin, diatoxanthin, diadinoxanthin, beta-carotene, and chlorophylls a and c characterized the diatom mats, whereas cyanobacterial mats contained myxoxanthophyll, zeaxanthin, echinenone, beta-carotene, chlorophyll a and, in some cases, sheath pigment. The presence of bacteriochlorophyll a within the mats suggest a close association of photosynthetic bacteria with diatoms and cyanobacteria. The high carotenoids : chlorophyll a ratios (0.84-2.44 wt/wt) in the diatom mats suggest that carotenoids served a photoprotective function in this high light environment. By contrast, cyanobacterial sheath pigment may have largely supplanted the photoprotective role of carotenoids in the intertidal mats.

Paracoccus halodenitrificans, grown anaerobically in the presence of nitrite, contained membrane and cytoplasmic nitrite reductases. When assayed in the presence of phenazine methosulfate and ascorbate, the membrane-bound enzyme produced nitrous oxide whereas the cytoplasmic enzyme produced nitric oxide. When both enzymes were assayed in the presence of methyl viologen and dithionite, the cytoplasmic enzyme produced ammonia. Following solubilization, the membrane-bound enzyme behaved like the cytoplasmic enzyme, producing nitric oxide in the presence of phenazine methosulfate and ascorbate, and ammonia when assayed in the presence of methyl viologen and dithionite. The cytoplasmic and membrane-bound enzymes were purified to essentially the same specific activity. Only a single nitrite-reductase activity was detected on electrophoretic gels and the electrophoretic behavior of both enzymes suggested they were identical. The spectral properties of both enzymes suggested they were cd-type cytochromes. These data suggest that the products of nitrite reduction by the cd-cytochrome nitrite reductase are determined by the location of the enzyme and the redox potential of the electron donor.