Mammalian cysteine dioxygenase (CDO) is a mononuclear non-heme iron protein that catalyzes 2 the conversion of cysteine (Cys) to cysteine sulfinic acid (CSA) by an unclarified mechanism. 3 One structural study revealed a Cys-persulfenate (or Cys-persulfenic acid) formed in the active 4 site, but quantum mechanical calculations have been used...
Full Text:
-bound 2
enzyme at higher pH 3
Camden M. Driggers
a
, Richard B. Cooley
a;b
, BanumathiSankaran
c
Mammalian cysteine dioxygenase (CDO) is a mononuclear non-heme iron protein that catalyzes 2 the conversion of cysteine (Cys) to cysteine sulfinic acid (CSA) by an unclarified mechanism. 3 One structural study revealed a Cys-persulfenate (or Cys-persulfenic acid) formed in the active 4 site, but quantum mechanical calculations have been used...
Mammalian cysteine dioxygenase (CDO) is a mononuclear non-heme iron protein that catalyzes 2 the conversion of cysteine (Cys) to cysteine sulfinic acid (CSA) by an unclarified mechanism. 3 One structural study revealed a Cys-persulfenate (or Cys-persulfenic acid) formed in the active 4 site, but quantum mechanical calculations have been used...
Sulfur is one of the six elements required during the early stages of the evolution of life, and enzymes involved in sulfur transfer and oxidation are increasingly being recognized as potential drug targets for antimicrobials as well as for therapies for cancer, neurodegenerative and inflammatory diseases. Bacteria are able to...
Peroxiredoxins (Prxs) are dominant peroxide-reducing enzymes with two important roles: they protect all organisms from oxidative damage induced by peroxides, and in eukaryotes, they participate in hydrogen peroxide signaling pathways. This dissertation presents studies aimed at the biophysical characterization of select Prxs and a Prx reductase to elucidate their structure-function...