Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli.

@article{Gladyshev1994CoordinationOS,
  title={Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli.},
  author={Vadim N. Gladyshev and Sergei V. Khangulov and Milton J. Axley and Thressa Campbell Stadtman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 16},
  pages={7708-11}
}
Formate dehydrogenase H from Escherichia coli contains multiple redox centers, which include a molybdopterin cofactor, an iron-sulfur center, and a selenocysteine residue (SeCys-140 in the polypeptide chain) that is essential for catalytic activity. Here we show that addition of formate to the native enzyme induces a signal typical of Mo(V) species. This signal is detected by electron paramagnetic resonance (EPR) spectroscopy. Substitution of 77Se for natural isotope abundance Se leads to… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 16 extracted citations

Selenium Toxic and Essential

View 20 Excerpts
Highly Influenced

Redox Pioneer: Professor Vadim N. Gladyshev.

Antioxidants & redox signaling • 2016
View 1 Excerpt

Similar Papers

Loading similar papers…