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Creator:: Driggers, Camden M., Cooley, Richard B., Sankaran, Banumathi, Hirschberger, Lawrence L., Stipanuk, Martha H., and Karplus, P. Andrew
Abstract:: 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...

Creator:: Driggers, Camden M., Cooley, Richard B., Sankaran, Banumathi, Hirschberger, Lawrence L., Stipanuk, Martha H., and Karplus, P. Andrew
Abstract:: 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...

Creator:: Driggers, Camden M., Cooley, Richard B., Sankaran, Banumathi, Hirschberger, Lawrence L., Stipanuk, Martha H., and Karplus, P. Andrew
Abstract:: 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...
Resource Type:: Article

ScholarsArchive@OSU