Vytas Reipa

NIST Building 227, Room A215
100 Bureau Drive
Gaithersburg, MD 20899-8312 USA
Phone: 301-975-5056
Email: vytas@nist.gov

Vytas Reipa

 

Education

  • Ph.D. Electrochemistry, Institute of Chemistry , Vilnius , Lithuania (1987)

Current Research

  • Biomolecule spectroscopy
  • electrochemistry
  • Si nanoparticles


Biomolecule spectroscopy, electrochemistry, Si nanoparticles.

Heterogeneous charge exchange between biomolecules and solid electrodes is the clean and quantitative way to control protein redox state. We are developing spectroelectrochemical methods for measuring the thermodynamic charge transfer equilibrium of biologically relevant reactions. The method was applied to the direct redox titration of desaturases, iron-sulfur proteins, cytochromes P450, flavoproteins and glutathione using absorbance, CD, fluorescence and Raman spectroscopy to measure degree of oxidation and structural variation.

We are exploring the applicability of the highly fluorescent Si nanoparticles.for biomolecule tagging. These particles offer biocompatibility, high quantum yields, photostability, and display emission in a wide spectral range. The current research focuses on developing methodologies for bioconjugation to DNR, proteins and stabilization of nanoparticles.

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Publications

  • “Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant D 9-18:0-acyl carrier protein desaturase”, V. Reipa, J. Shanklin, V.L. Vilker, Chemical Communications, Nov 7(21), 2406-2407 (2004).

  • “Temperature-induced structural changes in putidaredoxin: a circular dichroism and UV-VIS absorption study:, V. Reipa, M. J. Holden, M. P. Mayhew, V. L. Vilker, Biochimica et Biophysica Acta, 1699, 229-234 (2004).

  • “Direct spectroelectrochemical titration of glutathione”, V. Reipa, Bioelectrochemistry, 65, 47-49 (2004).

  • "Silicon Nanoparticles as a Luminescent label to DNA”, L. Wang, V. Reipa, J. Blasic, Bioconjugate Chemistry, 15, 409-412 (2004).

  • "Structural alterations of the heme environment of cytochrome P450cam and the Y96F mutant as deduced by resonance Raman spectroscopy”, G Niaura, V Reipa, MP Mayhew, M Holden, VL Vilker, Archives of Biochemistry and Biophysics, 409, 102-112 (2003).

  • "Redox Control Of The P450cam Catalytic Cycle: Effects Of Y96F Active Site Mutation And Binding Of A Non-Natural Substrate", V Reipa, MP Mayhew, MJ Holden and VL Vilker, Chemical Communications 4, 318-320 (2002).