Elucidating the behavior of an enzyme

Posted by / 07-May-2018 09:43

Elucidating the behavior of an enzyme

Unexpectedly, the uncharged SDH variants (R55Q and R55M) exhibited increased IET rate constants relative to that of the wild type (3-4-fold) when studied by laser flash photolysis.The gain in function observed in SDH(R55Q) and SDH(R55M) suggests that the reduction in the level of IET seen in HSO(R160Q) is not due to a required role of this residue in the IET pathway itself, but to the fact that it plays an important role in heme orientation during the interdomain movement necessary for IET in HSO (as seen in viscosity experiments).

This suggests that there is no significant subunit movement or a subunit “docking” step in SDH that could be retarded by a viscogen (18, 19), and that IET occurs through the protein and/or solvent interface between the two “locked” subunits which have a Mo···Fe distance of ~16 Å (7).Point mutations in the HSO structural gene that cause the disease phenotype generally result in conformational changes in and around the active site or the disruption of the dimeric structure of HSO to give inactive monomeric subunits.Active site mutations can affect the coordination of the molybdenum cofactor (Moco), the active site geometry, enzyme turnover rates, and cause decreased intramolecular electron transfer (IET) rates (15, 16).HSO deficiency is a rare recessive metabolic neurologic disorder that presents shortly after birth (9, 10).The disease is characterized by seizures, dislocated ocular lenses, neuropathogenesis, and early death most likely due to a combined effect of the accumulation of toxic sulfite and glutamate, decreased sulfate concentration, and oxidative stress (9, 11, 12, 13, 14).

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