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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Pyrococcus furiosus ferredoxin is a functional dimer
M N Hasan1, P L Hagedoorn, W R Hagen
1Kluyver Department of Biotechnology, Delft University of Technology, Delft, The Netherlands. m.n.hasan@tnw.tudelft.nl
Abstract:
Pyrococcus furiosus ferredoxin is subject to a monomer/dimer equilibrium as a function of ionic strength. At physiological ionic strength, approximately 0.35 M NaCl, the protein is very predominantly homodimer. The monomeric form exhibits impaired electron transfer on glassy carbon; it also has a decreased S=3/2 over S=1/2 ratio as shown by electron paramagnetic resonance spectroscopy. Even following sterilization at 121 degrees C the dimer is stable in denaturing gel electrophoresis.
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