Tools for on-demand protein activation enable impactful gain-of-function studies in biological settings. Thus far, however, proteins have been chemically caged at primarily Lys, Tyr, and Sec, typically through the genetic encoding of unnatural amino acids. Herein, we report that the preferential reactivity of diazo compounds with protonated acids can be used to expand this toolbox to solvent-accessible carboxyl groups with an elevated pK a value. As a model protein, we employed lysozyme (Lyz), which has an active-site Glu35 residue with a pK a value of 6.2. A diazo compound with a bioorthogonal self-immolative handle esterified Glu35 selectively, inactivating Lyz. The hydrolytic activity of the caged Lyz on bacterial cell walls was restored with two small-molecule triggers. The decaging was more efficient by small molecules than by esterases. This simple chemical strategy was also applied to a hemeprotein and an aspartyl protease, setting the stage for broad applicability.

Abstract. The activity of exploring natural oil and gas will produce gas flare 0.584 MMSCFD. A gas flare is the combustion of gas remaining to avoid poisonous gas like H 2 S and CO which is very dangerous for human and environmental health. The combustion can bring about environmental pollution and losses because it still contains valuable energy. It needs the policy to encourage the use of flare gas with Zero Routine Flaring and green productivity to reduce waste and pollution. The objective of the research was to determine the use of gas flare so that it will have economic value and can achieve Zero Routine Flaring. It was started by analysing based on volume or rate and composition gas flare was used to determine technical feasibility, and the estimation of the gas reserves as the determination of the economy of a gas well. The results showed that the use of flare gas as fuel for power generation feasible to be implemented technically and economically with Internal Rate of Return (IRR) 19.32% and the Payback Period (PP) 5 year. Thus, it can increase gas flare value economically and can achieve a breakthrough in Zero Routine Flaring.

I n the last two years, the science and policies surrounding COVID-19 vaccine development stood at the center of our lives, because they provided a clear escape route towards pre-pandemic normalcy. Now, from first-hand experience, we can fully grasp how critical it is for scientists, policymakers, and the public to communicate clearly, understand each other, and take collective action.

Tools for on-demand protein activation enable impactful gain-of-function studies in biological settings. Thus far, however, proteins have been chemically caged at primarily Lys, Tyr, and Sec, typically through the genetic encoding of unnatural amino acids. Herein, we report that the preferential reactivity of diazo compounds with protonated acids can be used to expand this toolbox to solvent-accessible carboxyl groups with an elevated pK a value. As a model protein, we employed lysozyme (Lyz), which has an active-site Glu35 residue with a pK a value of 6.2. A diazo compound with a bioorthogonal self-immolative handle esterified Glu35 selectively, inactivating Lyz. The hydrolytic activity of the caged Lyz on bacterial cell walls was restored with two small-molecule triggers. The decaging was more efficient by small molecules than by esterases. This simple chemical strategy was also applied to a hemeprotein and an aspartyl protease, setting the stage for broad applicability.

Oxoanions such as carboxylates, phosphates, and sulfates play important roles in both chemistry and biology and are abundant on the cell surface. We report on the synthesis and properties of a rationally designed guanidinium-containing oxoanion binder, 1-guanidino-8-amino-2,7-diazacarbazole (GADAC). GADAC binds to a carboxylate, phosphate, and sulfate in pure water with affinities of 3.6 × 104, 1.1 × 103, and 4.2 × 103 M–1, respectively. Like 2-azacarbazole, which is a natural product that enables scorpions to fluoresce, GADAC is fluorescent in water (λabs = 356 nm, λem = 403 nm, ε = 13,400 M–1 cm–1). The quantum yield of GADAC is pH-sensitive, increasing from Φ = 0.12 at pH 7.4 to Φ = 0.53 at pH 4.0 as a result of the protonation of the aminopyridine moiety. The uptake of GADAC into live human melanoma cells is detectable in the DAPI channel at low micromolar concentrations. Its properties make GADAC a promising candidate for applications in oxoanion binding and fluorescence labeling in biological (e.g., the delivery of cargo into cells) and other contexts.