Importance of Reaction Kinetics and Oxygen Crossover in aprotic Li-O2 Batteries Based on a Dimethyl Sulfoxide Electrolyte.

Although still in their embryonic state, aprotic rechargeable Li-O2 batteries have, theoretically, the capabilities of reaching higher specific energy densities than Li-ion batteries. There are, however, significant drawbacks that must be addressed to allow stable electrochemical performance; these will ultimately be solved by a deeper understanding of the chemical and electrochemical processes occurring during battery operations. We report a study on the electrochemical and chemical stability of Li-O2 batteries comprising Au-coated carbon cathodes, a dimethyl sulfoxide (DMSO)-based electrolyte and Li metal negative electrodes. The use of the aforementioned Au-coated cathodes in combination with a 1 M lithium bis(trifluoromethane)sulfonimide (LiTFSI)-DMSO electrolyte guarantees very good cycling stability (>300 cycles) by minimizing eventual side reactions. The main drawbacks arise from the high reactivity of the Li metal electrode when in contact with the O2 -saturated DMSO-based electrolyte.

Escherichia coli mutations that prevent the action of the T4 unf/alc protein map in an RNA polymerase gene.

Bacteriophage T4 has the substituted base hydroxymethylcytosine in its DNA and presumably shuts off host transcription by specifically blocking transcription of cytosine-containing DNA. When T4 incorporates cytosine into its own DNA, the shutoff mechanism is directed back at T4, blocking its late gene expression and phage production. Mutations which permit T4 multiplication with cytosine DNA should be in genes required for host shutoff. The only such mutations characterized thus far have been in the phage unf/alc gene. The product of this gene is also required for the unfolding of the host nucleoid after infection, hence its dual name unf/alc. As part of our investigation of the mechanism of action of unf/alc, we have isolated Escherichia coli mutants which propagate cytosine T4 even if the phage are genotypically alc+. These same E. coli mutants are delayed in the T4-induced unfolding of their nucleoid, lending strong support to the conclusion that blocking transcription and unfolding the host nucleoid are but different manifestations of the same activity. We have mapped two of the mutations, called paf mutations for prevent alc function. They both map at about 90 min, probably in the rpoB gene encoding a subunit of RNA polymerase. From the behavior of Paf mutants, we hypothesize that the unf/alc gene product of T4 interacts somehow with the host RNA polymerase to block transcription of cytosine DNA and unfold the host nucleoid.

Nucleotide and deduced amino acid sequence of stp: the bacteriophage T4 anticodon nuclease gene.

Pre-existing host tRNAs are reprocessed during bacteriophage T4 infection of certain Escherichia coli strains. In this pathway, tRNALys is cleaved 5' to the wobble base by anticodon nuclease and is later restored in polynucleotide kinase and RNA ligase reactions. Anticodon nuclease depends on prr, a locus found only in host strains that restrict T4 mutants lacking polynucleotide kinase and RNA ligase; and on stp, the T4 suppressor of prr restriction. stp was cloned and the nucleotide sequences of its wild-type and mutant alleles determined. Their comparison defined an stp open reading frame of 29 codons at 162.8 to 9 kb of T4 DNA (1 kb = 10(3) base-pairs). We suggest that stp encodes a subunit of anticodon nuclease, perhaps one that harbors the catalytic site; while additional subunits, such as a putative prr gene product, impart protein folding environment and tRNA substrate recognition.

Molecular proof that bacteriophage T4 alc and unf genes are the same gene.

The DNA of bacteriophage T4 normally has a substituted base, hydroxymethylcytosine, instead of the usual cytosine. The bacteriophage shuts off host transcription after infection presumably by specifically blocking transcription of cytosine DNA. If T4 incorporates cytosine into its own DNA, this shutoff mechanism is directed back at itself and blocks its own transcription. Mutations which overcome this transcriptional block are in the T4 alc gene, and alc mutations allow the propagation of T4 with cytosine in their DNA (L. Snyder, L. Gold, and E. Kutter, Proc. Natl. Acad. Sci. USA 73:3098-3102, 1976). By genetic criteria, alc is the same as another gene, unf, whose product is required for the unfolding of the bacterial nucleoid after infection (K. Sirotkin, J. Wei, and L. Snyder, Nature [London] 265:28-32, 1977; D. P. Snustad, M. A. Tigges, K. A. Parson, C. J. H. Bursch, F. M. Caron, J. F. Koerner, and D. J. Tutas, J. Virol. 17:622-641, 1976; M. Tigges, C. J. H. Bursch, and D. P. Snustad, J. Virol. 24:775-785, 1977). The product of the alc gene has been identified as a 19-kilodalton protein (R. E. Herman, N. Haas, and D. P. Snustad, Genetics 108:305-317, 1984; E. Kutter, R. Drivdahl, and K. Rand, Genetics 108:291-304, 1984), and an open reading frame has been proposed to be the alc gene based on its size and map position (E. Kutter, R. Drivdahl, and K. Rand, Genetics 108:291-304, 1984). We used marker rescue techniques and DNA sequencing to confirm that this open reading frame is the alc gene. We also present a molecular proof that alc and unf are the same gene. While these results do not rigorously exclude the possibility that Unf and Alc are different activities of the same protein, they strongly support the conclusion that the unfolding of the bacterial nucleoid the blockage of transcription are but different manifestations of the same activity.