Persistent symptoms after COVID-19: an Australian stratified random health survey on long COVID.

Objective: To determine the impact of persistent symptoms after coronavirus disease 2019 (COVID-19) in an Australian population.

Design, Setting, Participants: We conducted a statewide health survey of a stratified random sample of adults who had had a confirmed acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection (COVID-19-positive group) and their close contacts (control group). The sample was drawn from Victoria's COVID-19 database between January 2020 and October 2022.

A comparison of marker gene selection methods for single-cell RNA sequencing data.

Background: The development of single-cell RNA sequencing (scRNA-seq) has enabled scientists to catalog and probe the transcriptional heterogeneity of individual cells in unprecedented detail. A common step in the analysis of scRNA-seq data is the selection of so-called marker genes, most commonly to enable annotation of the biological cell types present in the sample. In this paper, we benchmark 59 computational methods for selecting marker genes in scRNA-seq data.

New insights into controlling radical migration pathways in heme enzymes gained from the study of a dye-decolorising peroxidase.

In heme enzymes, such as members of the dye-decolorising peroxidase (DyP) family, the formation of the highly oxidising catalytic Fe(iv)-oxo intermediates following reaction with hydrogen peroxide can lead to free radical migration (hole hopping) from the heme to form cationic tyrosine and/or tryptophan radicals. These species are highly oxidising (∼1 V NHE) and under certain circumstances can catalyse the oxidation of organic substrates. Factors that govern which specific tyrosine or tryptophan the free radical migrates to in heme enzymes are not well understood, although in the case of tyrosyl radical formation the nearby proximity of a proton acceptor is a recognised facilitating factor.

Iron Oxidation in Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with HO but Slowly with O.

Both O and HO can oxidize iron at the ferroxidase center (FC) of bacterioferritin (EcBfr) but mechanistic details of the two reactions need clarification. UV/Vis, EPR, and Mössbauer spectroscopies have been used to follow the reactions when apo-EcBfr, pre-loaded anaerobically with Fe, was exposed to O or HO. We show that O binds di-Fe FC reversibly, two Fe ions are oxidized in concert and a HO molecule is formed and released to the solution.

Electron Transfer from Haem to the Di-Iron Ferroxidase Centre in Bacterioferritin.

The iron redox cycle in ferritins is not completely understood. Bacterioferritins are distinct from other ferritins in that they contain haem groups. It is acknowledged that the two iron motifs in bacterioferritins, the di-nuclear ferroxidase centre and the haem B group, play key roles in two opposing processes, iron sequestration and iron mobilisation, respectively, and the two redox processes are independent.