Their versatility, which arises from an ability to undergo reduction-oxidation chemistry, enables them to act as critical cofactors of enzymes throughout the cell.

Reactive oxygen species, generated by reduction-oxidation (redox) reactions, have been recognized as one of the major mediators of ischemia and reperfusion injury in the brain.

Reduction-oxidation (redox) signaling systems are emerging as important targets in pancreatic cancer.

Iron-sulfur clusters are prosthetic groups commonly found in proteins that participate in oxidation-reduction reactions and catalysis.

The N-terminus of MTRR containing a conserved domain of FMNRed is closely concerned with the oxidation-reduction process.

The mutated proteins show spectral properties similar to those of the wild-type enzyme, in all oxidation-reduction states.

This is in accord with the high oxidation-reduction potential of the flavin, which thermodynamically stabilizes the reduced enzyme.

In comparison, 27 proteins were up-regulated in dark-cutting beef related to oxidation-reduction processes, muscle contraction, and oxidative phosphorylation.

This cyclic redox reaction of the metal generates OH.

Taken together these data demonstrate that H296 is responsible for proton exchange in the redox reaction.

Flavin-based electron-bifurcation is a mechanism that couples an exergonic redox reaction to an endergonic one allowing energy conservation in anaerobic microorganisms.

This provides mass spectrometric evidence for the mechanism of the nitro to amine conversion process during nitroreduction, an important redox reaction involved in carcinogenesis.

Re-evaluating these previous data we here discuss a mechanism, by which the redox reaction of N2 induces conformational changes possibly leading to proton translocation.