Research >> Oxidative Stress
smitra@bu.edu
|
|
Sangha Mitra, Ph.D. Senior Research Associate, Dept of Molecular and Cell biology Thioredoxin (Trx) and
glutaredoxin (Grx) belong to Trx superfamily of thioldisulfide oxidoreductases. These
are small soluble proteins sharing a single -CXXC- motif that contains the cysteine
residues participating in the 2e-/2H+ chemistry. It has been suggested that
the nature of the amino acids in the motif determines the reduction potential
of the resulting disulfide. I have installed -CXXC- sequences of known
oxidizing and reducing disulfide bonds in an identical Trx protein fold and
have used protein film voltammometry (PFV) to determine their reduction
potentials. My results reveal a connection between sequence and redox
potentials. Recently, human Grx2 in
its inactive dimeric form was found to contain an iron-sulfur cluster and was
proposed to function as a redox sensor. I have produced the iron-sulfur
loaded form of the protein, and have used PFV to induce and monitor the
impact of oxidative stress on the ironsulfur cluster in a recombinant human
Grx2. Related Publications: 1. Mitra, S. and Elliott, S. J. “Oxidative disassembly of the [2Fe-2S] cluster in human Grx-2: redox regulation in the mitochondria.” Chem Biochem (communication), (submitted). |
