Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH‐binding properties
Low‐molecular‐weight (low Mr) thioredoxin reductases (TrxRs) are homodimeric NADPH‐dependent dithiol flavoenzymes that reduce thioredoxins (Trxs) or Trx‐like proteins involved in the activation networks of enzymes, such as the bacterial class Ib ...
Marita Shoor +3 more
doaj +1 more source
Crystallization and preliminary diffraction studies of morphinone reductase, a flavoprotein involved in the degradation of morphine alkaloids [PDF]
Morphinone reductase from Pseudomonas putida M10, a flavoprotein involved in the degradation of morphine alkaloids, was purified from an overexpressing strain of Escherichia coli and crystallized using the hanging-drop vapour-diffusion method ...
Bruce, N C +4 more
core +1 more source
Cell wall target fragment discovery using a low‐cost, minimal fragment library
LoCoFrag100 is a fragment library made up of 100 different compounds. Similarity between the fragments is minimized and 10 different fragments are mixed into a single cocktail, which is soaked to protein crystals. These crystals are analysed by X‐ray crystallography, revealing the binding modes of the bound fragment ligands.
Kaizhou Yan +5 more
wiley +1 more source
The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes
Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit.
Filipa Calisto +3 more
doaj +1 more source
Human Heme Oxygenase Oxidation of 5- and 15-Phenylhemes [PDF]
Human heme oxygenase-1 (hHO-1) catalyzes the O2- dependent oxidation of heme to biliverdin, CO, and free iron. Previous work indicated that electrophilic addition of the terminal oxygen of the ferric hydroperoxo complex to the -meso-carbon gives 5 ...
Alvarez, Diego Ezequiel +7 more
core +1 more source
Structural biology of ferritin nanocages
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley +1 more source
Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein [PDF]
Copper has an important role in the life cycle of many streptomycetes, stimulating the developmental switch between vegetative mycelium and aerial hyphae concomitant with the production of antibiotics.
Calabrese L +5 more
core +2 more sources
We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley +1 more source
Enzymology of retinoic acid biosynthesis and degradation
All-trans-retinoic acid is a biologically active derivative of vitamin A that regulates numerous physiological processes. The concentration of retinoic acid in the cells is tightly regulated, but the exact mechanisms responsible for this regulation are ...
Natalia Y. Kedishvili
doaj +1 more source
Erythrocyte Glutathione Reductase [PDF]
Abstract 1. The physiologic roles of glutathione in the red cell and of glutathione reductase are reviewed briefly. 2. The partial purification of glutathione reductase by a combination of salting out, heating and chromatographic procedures is described. 3.
E, BEUTLER, M K, YEH
openaire +2 more sources

