TL;DR: These resting state and inhibited humanCatalase structures support specific, structure-based mechanisms for the catalase substrate recognition, reaction and inhibition and provide a molecular basis for understanding ethanol intoxication and the likely effects of human polymorphisms.
TL;DR: These findings confirm the recent description of the membrane-bound cytochrome b as a FAD-containing flavocy tochrome b containing the NADPH binding site, and implicate the three cytosolic proteins in its activation.
TL;DR: New details of NADPH binding to Lactobacillus casei dihydrofolate reductase have become visible as a result of crystallographic refinement to an R factor of 0.152 at 1.7 A resolution.
TL;DR: The results suggest that thioredoxin reductase must undergo conformational changes during enzyme catalysis, and no direct evidence is available as yet for such conformational change.
TL;DR: The activation domain of p67 phox regulates the reduction of FAD but has only a small effect on NADPH binding, consistent with a dominant effect on hydride/electron transfer from NADPH to FAD.