Alone in the COVID-19 lockdown : An exploratory study

Feelings of isolation have been prevalent worldwide since March 2020 due to COVID-19 pandemic lockdowns. This has prompted increased concerns about loneliness and related mental health problems. During the first UK COVID-19 lockdown, 71 participants were asked to share their high and low point stories from lockdown. These were analyzed using thematic analysis to explore how “aloneness” was experienced at this time. A deductive analyses supported three key facets of aloneness reported in the literature: emotional loneliness, social loneliness, and existential loneliness, as well as a more positive form of aloneness, solitude. An inductive analysis identified risk and protective factors for loneliness, comprising worry, lockdown changes, and poor mental health; and social contact, emotional contact, stability and simple life. The study highlights the importance of understanding how facets of aloneness interrelate, and how understanding risk and protective factors can help us to develop social and policy interventions to alleviate loneliness. In particular, solitude is proposed as a potential mechanism for alleviating loneliness, particularly existential loneliness, alongside more common social methods

A Conserved Mechanism for Sulfonucleotide Reduction

Sulfonucleotide reductases are a diverse family of enzymes that catalyze the first committed step of reductive sulfur assimilation. In this reaction, activated sulfate in the context of adenosine-5′-phosphosulfate (APS) or 3′-phosphoadenosine 5′-phosphosulfate (PAPS) is converted to sulfite with reducing equivalents from thioredoxin. The sulfite generated in this reaction is utilized in bacteria and plants for the eventual production of essential biomolecules such as cysteine and coenzyme A. Humans do not possess a homologous metabolic pathway, and thus, these enzymes represent attractive targets for therapeutic intervention. Here we studied the mechanism of sulfonucleotide reduction by APS reductase from the human pathogen Mycobacterium tuberculosis, using a combination of mass spectrometry and biochemical approaches. The results support the hypothesis of a two-step mechanism in which the sulfonucleotide first undergoes rapid nucleophilic attack to form an enzyme-thiosulfonate (E-Cys-S-SO(3) (−)) intermediate. Sulfite is then released in a thioredoxin-dependent manner. Other sulfonucleotide reductases from structurally divergent subclasses appear to use the same mechanism, suggesting that this family of enzymes has evolved from a common ancestor