Cookies Policy

This site uses cookies. By continuing to browse the site you are agreeing to our use of cookies.

I accept this policy

Find out more here

Photoinduced Electron and Hole Transfer Involving Eosin Conjugates of Tryptophan Derivatives

No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.

Brill’s MyBook program is exclusively available on BrillOnline Books and Journals. Students and scholars affiliated with an institution that has purchased a Brill E-Book on the BrillOnline platform automatically have access to the MyBook option for the title(s) acquired by the Library. Brill MyBook is a print-on-demand paperback copy which is sold at a favorably uniform low price.

Access this article

+ Tax (if applicable)
Add to Favorites
You must be logged in to use this functionality

image of Research on Chemical Intermediates

The preparation of several covalent conjugates of the dye, eosin Y (EY2-) with the amino acid, L-tryptophan (Trp), the dipeptide, Trp-Trp, and with poly(L)-tryptophan is described. Intramolecular photochemical electron transfer is responsible for the quenching of dye excited singlet states (flourescence) in these systems. The sacrificial acceptor, tetranitromethane (TNM), was used to irreversibly oxidize pendant dye groups; the transfer of charge ("holes") from the oxidized eosin moiety located at the N-terminus of the peptides was monitored by laser flash photolysis. Both modes of electron transfer involve charge transfer from indole side chains associated with Trp groups for the various peptide links. Study of the kinetics of hole transfer provided rate constants in the range of 103-104 s-1 for several solvent media including aqueous poly(vinylpyrrolidinone) (PVP), a polymer that provides a protein-like microdomain. The observed temperature dependence of the hole transfer rate is consistent with non-adiabatic electron transfer over distances determined by molecular modeling to be about 1.0 nm (through-space) and involving through-bond interactions via a network of σ-π overlaps. Findings are discussed in terms of demonstration of the entrainment of charge along peptide chains and the efficient separation of charge in (bio)polymer structures of some size that display vectorial properties.

Affiliations: 1: Department of Chemistry, Boston University, Boston MA 02215 USA


Full text loading...


Data & Media loading...

Article metrics loading...



Can't access your account?
  • Tools

  • Add to Favorites
  • Printable version
  • Email this page
  • Subscribe to ToC alert
  • Get permissions
  • Recommend to your library

    You must fill out fields marked with: *

    Librarian details
    Your details
    Why are you recommending this title?
    Select reason:
    Research on Chemical Intermediates — Recommend this title to your library
  • Export citations
  • Key

  • Full access
  • Open Access
  • Partial/No accessInformation