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These can include the rational redesign of membrane-bound enzymes to produce soluble catalysts 60 or the use of novel non-mammalian enzymes 61

Interestingly, AKT2/3 can either be strongly voltage-dependent being activated by increasingly negative membrane potentials (but being inactive around the K + Nernst potential), or it can operate in a voltage-independent mode with K + channel activity being unaffected by the membrane potential (Dreyer et al., Reference Dreyer, Michard, Lacombe and Thibaud2001)

All NADPH oxidase isoforms share a common structural homology, featuring a catalytic core composed of six transmembrane helices chelating two hemes and a dehydrogenase domain (DH) that binds the non-covalently linked flavin cofactor (FAD) and the NADPH substrate [25]