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Search Publications by: Vytas Reipa (Fed)

Displaying 76 - 100 of 137

Direct spectroeletrochemical titration of glutathione.

July 1, 2005

Author(s)

Vytautas Reipa

Infrared and Raman Spectroscopy Characterization of Biological Products

January 1, 2005

Author(s)

Vytautas Reipa

Both infrared and Raman are increasingly applied in biomolecular structure characterization, thus getting acceptance alongside traditional bioanalytical techniques. Physical principles and biological sampling requirements are reviewed. Advanced

Direct Spectroelectrochemical Titration of Glutathione

December 1, 2004

Author(s)

Vytautas Reipa

Spectroelectrochemistry measurements are used to determine the formal potential E of glutathione. Nernst titration was performed by monitoring disulfide absorption at 258 nm in a thin layer cell. Use of nanocrystalline highly doped tin oxide electrodes

Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant D(9)-18:0-acyl carrier protein desaturase

September 23, 2004

Author(s)

Vytautas Reipa, J Shanklin, V L. Vilker

Structural Changes that Accompany the Temperature Dependence of the Formal Potential of Putidaredoxin

June 1, 2004

Author(s)

Vytautas Reipa, Marcia J. Holden, M P. Mayhew, V L. Vilker

Temperature-induced structural changes in putidaredoxin: a circular dichroism and UV-VIS absorption study

June 1, 2004

Author(s)

Vytautas Reipa, Marcia J. Holden, M P. Mayhew, V L. Vilker

Temperature-Induced Structural Changes in Putidaredoxin: A Circular Dichroism and UV-VIS Absorption Study

June 1, 2004

Author(s)

Vytautas Reipa, Marcia J. Holden, M P. Mayhew, V L. Vilker

Putidaredoxin (Pdx) is an 11,400 Da iron-sulfur protein that sequentially transfers two electrons to the cytochrome P450cam during the enzymatic cycle of the stereo specific camphor hydroxylation. We report two transitions in the Pdx UV-VIS absorption and

Structural Alterations of the Heme Environment of Cytochrome P450cam and the Y96F Mutant as Deduced by Resonance Raman Spectroscopy

January 1, 2003

Author(s)

G Niaura, Vytas Reipa, M P. Mayhew, Marcia J. Holden, V L. Vilker

Resonance Raman spectroscopy at 2.5 cm-1 resolution was used to probe differences in wild type and Y96F mutant P450cam (CYP101), both with and without bound camphor or styrene substrates. In the substrate-free state, the spin state equilibrium is shifted

New Degenerate Metal-Oxide Electrodes for Nearly Reversible Direct Electron Transfer to the Redox Proteins

April 1, 2002

Author(s)

Gintaras Valincius, Vytautas Reipa, M P. Mayhew, V L. Vilker

Heavily doped cadmium tin oxide (CTO) film electrodes were developed for fast electron exchange with redox proteins. The metal oxide films showed nearly reversible electron transfer for the [2Fe-2S] proteins spinach ferredoxin (Sp fd) and putidaredoxin

Redox Control of the P450cam Catalytic Cycle: Effects of Y96F Active Site Mutation and Binding of a Non-Natural Substrate

January 1, 2002

Author(s)

Vytautas Reipa, M P. Mayhew, Marcia J. Holden, V L. Vilker

Spectroelectrochemical measurements are used to demonstrate that active site mutation and binding of a non-natural substrate to P450cam (CYP101) reduces the shift in the redox potential caused by substrate-binding, and thereby results in slower catalytic

Electrochemical Properties of Nanocrystalline Cadmium Stannate Films

August 1, 2001

Author(s)

Gintaras Valincius, Vytas Reipa, V L. Vilker, John T. Woodward IV, Mark D. Vaudin

Electrochemical properties of the sol-gel nanocrystalline cadmium tin oxide electrodes (CTO) were investigated in 0.2 M potassium chloride buffered at pH 7.4 with phosphate. Films were found to be n-type degenerate semiconductors with charge carrier levels

Electrochemical Properties of Nanocrystalline Cadmium Stannate Films

August 1, 2001

Author(s)

Gintaras Valincius, Vytautas Reipa, V L. Vilker, John T. Woodward IV, Mark D. Vaudin

Temperature Dependence of the Formal Reduction Potential of Putidaredoxin

July 20, 2000

Author(s)

Vytautas Reipa, Marcia J. Holden, M P. Mayhew, V L. Vilker

Putidaredoxin (Pdx), a [2Fe-2S] redox protein of size M r transfers two electrons in two separate steps from the flavin containing putidaredoxin reductase to the heme protein, cytochrome CYP101 in the P450cam catalytic cycle. It has recently come to light