PubMed · 5823521
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L F Saylor. 1969. Chloramphenicol--another warning.. https://pubmed.ncbi.nlm.nih.gov/5823521/
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The extensive use of chloramphenicol (CAP) in livestock leads the accumulation of CAP in livestock manures, threatening environmental and human health. Therefore, eliminating or reducing CAP concentration in manures before its re-utilization and application through microbial remediation is necessary. Exiguobacterium sp. CAP4, isolated from the plastisphere in duck manures, was capable of degrading CAP with the biodegradation efficiency of 97.8 % at initial CAP concentration of 5 mg/L within 4 days. A total of twenty-four biotransformation products were determined, including two novel transformation products, TP166 and TP203, enriched the integrity of CAP biodegradation pathways. Furthermore, the biotransformation process was proposed as a detoxifying process through biotransformation products toxicity evaluation. Notably, Exiguobacterium sp. CAP4 successfully colonized in the cow manures after inoculation, and bioaugmented the biodegradation of CAP in virgin cow manures. This study significantly extended our understanding of the CAP biotransformation fate, and provided a promising bacterial strain for bioremediation of CAP containing wastewater in situ.
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Mutants of the cyanobacterium Synechocystis PCC 6803 lacking the psbO or psbH gene are more vulnerable to photoinhibition than the wild type (WT). In the case of the psbO-less mutant, the increased sensitivity to photodamage is also accompanied by accelerated turnover of the D1 protein and a rapid rate of recovery on transfer to non-photoinhibitory conditions. In contrast, in low light the psbH-less mutant has a poor ability to recover after photoinhibition and has a reduced rate of D1 turnover as compared with WT. Since the psbO gene encodes the 33 kDa manganese-stabilizing protein associated with the water-splitting reaction, the increased sensitivity to photoinduced damage is attributed to perturbation of electron transfer processes on the donor side of photosystem II (PSII). In contrast, the absence of H protein, encoded by the psbH gene, affects the acceptor side of PSII with preferential photoinhibitory damage occurring at the QB site. The apparent consequence of this is that the psbH-less mutant, unlike the psbO-less mutant, is not able to regulate the rate of turnover of the D1 protein. In all cases it was shown that chloramphenicol, which blocks protein synthesis, enhances the rate of photoinhibition as judged by a decrease in oxygen evolution but slows down the rate of degradation of D1 protein compared to that observed during normal turnover.(ABSTRACT TRUNCATED AT 250 WORDS)