1. Rapid preparation of gaseous methanediol (CH2(OH)2)
Yi-Fang Chen, Li-Kang Chu Chem Commun (Camb). 2022 Mar 29;58(26):4208-4210. doi: 10.1039/d2cc00964a.
The simplest geminal diol CH2(OH)2 serves as an important precursor to form atmospheric formic acid. CH2(OH)2 vapour can be generated by the evaporation of an aqueous formaldehyde solution, prepared by dissolving paraformaldehyde under reflux. Its rovibrational feature at 980-1100 cm-1 is consistent with the simulation and free of the intense interferences of H2O and CH2O.
2. NH2OH Disproportionation Mediated by Anaerobic Ammonium-oxidizing (Anammox) Bacteria
Mamoru Oshiki, Lin Gao, Lei Zhang, Satoshi Okabe Microbes Environ. 2022;37(2):ME21092. doi: 10.1264/jsme2.ME21092.
Anammox bacteria produce N2 gas by oxidizing NH4+ with NO2-, and hydroxylamine (NH2OH) is a potential intermediate of the anammox process. N2 gas production occurs when anammox bacteria are incubated with NH2OH only, indicating their capacity for NH2OH disproportionation with NH2OH serving as both the electron donor and acceptor. Limited information is currently available on NH2OH disproportionation by anammox bacteria; therefore, the stoichiometry of anammox bacterial NH2OH disproportionation was examined in the present study using 15N-tracing techniques. The anammox bacteria, Brocadia sinica, Jettenia caeni, and Scalindua sp. were incubated with the addition of 15NH2OH, and the production of 15N-labeled nitrogenous compounds was assessed. The anammox bacteria tested performed NH2OH disproportionation and produced 15-15N2 gas and NH4+ as reaction products. The addition of acetylene, an inhibitor of the anammox process, reduced the activity of NH2OH disproportionation, but not completely. The growth of B. sinica by NH2OH disproportionation (-240.3 kJ mol NH2OH-1 under standard conditions) was also tested in 3 up-flow column anammox reactors fed with 1) 0.7 mM NH2OH only, 2) 0.7 mM NH2OH and 0.5 mM NH4+, and 3) 0.7 mM NH2OH and 0.5 mM NO2-. NH2OH consumption activities were markedly reduced after 7 d of operation, indicating that B. sinica was unable to maintain its activity or biomass by NH2OH disproportionation.
3. The Dual Role of the 2'-OH Group of A76 tRNATyr in the Prevention of d-tyrosine Mistranslation
Mariia Yu Rybak, Oksana P Kovalenko, Michael A Tukalo J Mol Biol. 2018 Aug 17;430(17):2670-2676. doi: 10.1016/j.jmb.2018.06.036. Epub 2018 Jun 25.
Aminoacyl-tRNA-synthetases are crucial enzymes for initiation step of translation. Possessing editing activity, they protect living cells from misincorporation of non-cognate and non-proteinogenic amino acids into proteins. Tyrosyl-tRNA synthetase (TyrRS) does not have such editing properties, but it shares weak stereospecificity in recognition of d-/l-tyrosine (Tyr). Nevertheless, an additional enzyme, d-aminoacyl-tRNA-deacylase (DTD), exists to overcome these deficiencies. The precise catalytic role of hydroxyl groups of the tRNATyr A76 in the catalysis by TyrRS and DTD remained unknown. To address this issue, [32P]-labeled tRNATyr substrates have been tested in aminoacylation and deacylation assays. TyrRS demonstrates similar activity in charging the 2' and 3'-OH groups of A76 with l-Tyr. This synthetase can effectively use both OH groups as primary sites for aminoacylation with l-Tyr, but demonstrates severe preference toward 2'-OH, in charging with d-Tyr. In both cases, the catalysis is not substrate-assisted: neither the 2'-OH nor the 3'-OH group assists catalysis. In contrast, DTD catalyzes deacylation of d-Tyr-tRNATyr specifically from the 3'-OH group, while the 2'-OH assists in this hydrolysis.
