A useful tool for disulfide bridges reduction, for example in proteins, is DTT. As a product of these reductions (in attachment) we have an "oxidized DTT" (http://www.sigmaaldrich.com/catalog/product/aldrich/d3511). Does anyone have knowledge of its RAMAN spectum or any ideas about it?
In the database
http://sdbs.riodb.aist.go.jp/sdbs/cgi-bin/cre_index.cgi?lang=eng
searching for dithiane, you can find the IR of such a compound.
Anyway, I think that if you are interested in distinguishing the oxidized S-S in protein (reactant) from the oxidized DTT (product), Raman is not the best choice. If you use Raman, probably, a better reducing agent is TCEP tris(2-carboxyethyl)phosphine, (no overlap in the 500-550 cm-1 region).
Thank you again. I found out, that oxidized DTT certainly has a huge raman peak on 516 (David C. et al. Reductive Unfolding of Serum Albumins, Biopolymers Volume 89 / Number 7). Of course, there is still a possibility to analize the protein SS bridges changes using component decomposition
If anyone is interested, there is also a Raman spectrum of trans-4,5-Dihydroxy-1,2-dithiane (oxidized DTT) in the proprietary Raman library "HR Aldrich Raman".
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