Intermediary Metabolism and Bioenergetics Section
Thressa C Stadtman, PhD, Principal Investigator
Major projects include the following: (1) Selenophosphate synthetase;
biological Se substrate and mechanism of action. (2) Mammalian
thioredoxin reductase; structure, mechanism of action, role of
Secys. (3) Identity and function of 33 kDa Se-binding protein
from Methanococcus vannielii.
For more information, please contact Thressa
C Stadtman.
![Proposed reactions for the formation of protein perselenide and pathways for selenophosphate formation. Cysteine-free rhodanese-type enzyme is shown as a protein (S ). Se*, an unidentified transfer form of selenium.](https://webarchive.library.unt.edu/eot2008/20090113182938im_/http://dir.nhlbi.nih.gov/labs/lb/images/Perselenide.jpg) |
Proposed reactions for the formation
of protein perselenide and pathways for selenophosphate formation.
Cysteine-free rhodanese-type enzyme is shown as a protein
(S ). Se*, an unidentified transfer form of selenium. Read
more.![PDF file](https://webarchive.library.unt.edu/eot2008/20090113182938im_/http://dir.nhlbi.nih.gov/labs/lb/images/pdfsmall.gif) |
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