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Chemicals, plastics and rubber industries

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Long-ranged electron interaction between carboxytetramethylrhodamine and fluoresceinisothiocyanate bound covalently to DNA, as evidenced by fluorescence quenching

Article Abstract:

A study was conducted to analyze the fluorescence of 5-carboxytetramethylrhodamine and fluoresceinisothiocyanate bound to double-stranded DNA residues using steady-state and time-resolved fluorescence measurements. Results indicated that the quenching of fluorescence correlated with the transfer of electrons from the dye to DNA. Findings also confirmed the presence of electron transfer interaction between two dye molecules bound to both ends of long dsDNA.

Author: Kojima, Hiroyuki, Spataru, Nicolae, Kawata, Yoshikazu, Yano, Sin-ichi, Vartires, Iuliana
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
Research, DNA, Fluorescence, Molecular dynamics

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The effect of ionic strength on the electron-transfer rate of surface immobilized cytochrome c

Article Abstract:

Horse heart cytochrome c is immobilized on four different self-assembled monolayer (SAM) films and cyclic voltammetry is used to analyze the electron tunneling kinetics in different assemblies as a function of the ionic strength of the buffer solution. The observed inhomogeneity indicates that a distribution of cytochrome c orientations and hence a distribution of electron transfer rate constants exists.

Author: Waldeck, David H., Petrovic, Jelena, Clark, Rose A.
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
Analysis, Design and construction, Electron transport, Monomolecular films

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Structural character and energetics of tyrosyl radical formation by electron/proton transfer of a covalently linked histidine-tyrosine: A model for cytochrome c oxidase

Article Abstract:

The structural, energetic, electronic and infrared (IR) spectroscopic properties for a model of the cross-linked histidine-tyrosine (His-Tyr) residues as found in the cytochrome c oxidase (CcO) were investigated by ab initio methods. The results demonstrated that the cationized cross-linked His-Tyr is the best prospect to mimic the covalently ring-linked His-Tyr structure in CcO.

Author: Yuxiang Bu, Cukier, R.I.
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2005
Histidine, Tyrosine

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Subjects list: Cytochrome c, Atomic properties
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