Diatoms encode two forms of flavodoxin with divergent functions that mitigate the oxidative stress and iron requirements associated with life in contemporary oxygenated iron-poor oceans.

Like two peas in a pod but not exactly alike, similar molecules targeting the same bacterial protein behave differently, requiring systems biology and target deconvolution to gain better comprehension.

Bioinformatic and biochemical studies provide evidence that covalently bound flavins are common and participate in wide-ranging extracytosolic redox activities throughout bacterial life.

The intracellular network that distributes iron-sulfur clusters in bacteria is surprisingly 'plug and play' with iron-sulfur enzymes acquired from distantly related species, whereas the intracellular electron transfer network often needs plug adapters to connect with foreign enzymes.

Synechocystis switches its redox pools under reducing photomixotrophic conditions from utilizing NAD(H)- to ferredoxin-dependent enzymes and thereby balances its metabolism in a trade-off between energy conservation and chemical driving forces.

Directed evolution of the resistance enzyme Cfr under antibiotic selection identifies increased Cfr expression and stability as strategies to boost resistance and reveals that Cfr modification of the ribosome confers resistance by sterically occluding binding of antibiotics.

Analysisof P-loop NTPases and Rossmans, the most ancient and diverse enzyme lineages, suggests their divergence from one ancestral polypeptide.

In vivo evidence is provided indicating that Flv2/Flv4, together with Flv1/Flv3, mediate O₂ photoreduction downstream of PSI in a highly coordinated manner.

The flavoprotein NrdI in class Ib ribonucleotide reductase controls superoxide generation and metal site oxidation by tuning the redox properties of its flavin cofactor via steric strain induced by the formation of the R2b–NrdI protein complex.