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Relevant bibliographies by topics / Biology - Electron Transfer

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Academic literature on the topic 'Biology - Electron Transfer'

Author: Grafiati

Published: 7 September 2023

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Journal articles on the topic "Biology - Electron Transfer"

1

Williams, R. J. P. "Electron transfer in biology." Molecular Physics 68, no. 1 (September 1, 1989): 1–23. http://dx.doi.org/10.1080/00268978900101931.

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Sledow, James N., and Ann L. Umbach. "Plant Mitochondrial Electron Transfer and Molecular Biology." Plant Cell 7, no. 7 (July 1995): 821. http://dx.doi.org/10.2307/3870039.

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Agapakis, Christina M., and Pamela A. Silver. "Modular electron transfer circuits for synthetic biology." Bioengineered Bugs 1, no. 6 (November 2010): 413–18. http://dx.doi.org/10.4161/bbug.1.6.12462.

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Matyushov, Dmitry V. "Protein electron transfer: is biology (thermo)dynamic?" Journal of Physics: Condensed Matter 27, no. 47 (November 12, 2015): 473001. http://dx.doi.org/10.1088/0953-8984/27/47/473001.

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Blankenship, Robert E. "Protein electron transfer." FEBS Letters 398, no. 2-3 (December 2, 1996): 339. http://dx.doi.org/10.1016/0014-5793(97)81275-6.

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Moser, Christopher C., Christopher C. Page, Ramy Farid, and P. Leslie Dutton. "Biological electron transfer." Journal of Bioenergetics and Biomembranes 27, no. 3 (June 1995): 263–74. http://dx.doi.org/10.1007/bf02110096.

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Rivas, Maria Gabriela, Pablo Javier Gonzalez, Felix Martin Ferroni, Alberto Claudio Rizzi, and Carlos Brondino. "Studying Electron Transfer Pathways in Oxidoreductases." Science Reviews - from the end of the world 1, no. 2 (March 16, 2020): 6–23. http://dx.doi.org/10.52712/sciencereviews.v1i2.15.

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Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.

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Parsons, Roger. "Electron transfer in biology and the solid state." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 305, no. 1 (April 1991): 166. http://dx.doi.org/10.1016/0022-0728(91)85214-a.

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Berg, Hermann. "Electron and Proton Transfer in Chemistry and Biology." Bioelectrochemistry and Bioenergetics 32, no. 1 (September 1993): 97–98. http://dx.doi.org/10.1016/0302-4598(93)80027-r.

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Holtzhauer, Martin, and Peter Mohr. "Electron and Proton Transfer in Chemistry and Biology." Zeitschrift für Physikalische Chemie 186, Part_1 (January 1994): 119. http://dx.doi.org/10.1524/zpch.1994.186.part_1.119.

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Dissertations / Theses on the topic "Biology - Electron Transfer"

1

Lee, Lester Y. C. "Transmembrane electron transfer in artificial bilayers /." Full text open access at:, 1985. http://content.ohsu.edu/u?/etd,86.

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Danyal, Karamatullah. "Electron Transfer and Substrate Reduction in Nitrogenase." DigitalCommons@USU, 2014. https://digitalcommons.usu.edu/etd/2181.

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Population growth over the past ~50 years accompanied by the changes in dietary habits due to economic growth have markedly increased the demand for fixed nitrogen. Aided by biological nitrogen fixation, the Haber-Bosch process has been able to fulfill these demands. However, due to its high temperature and pressure requirements, Haber-Bosch is an expensive process. Every year, approximately 2% of the total energy expenditure by man is used to manufacture fixed nitrogen. Biological systems, on the other hand, produce ammonia at ambient temperature and pressure with much higher efficiency than the Haber-Bosch process. Research in the field of biological nitrogen fixation could prove valuable in understanding the mechanism of the enzyme responsible, nitrogenase. This could eventually allow researchers to mimic the enzyme and fix nitrogen at standard temperature and pressure, which would lead to greater availability of fixed nitrogen and a better standard of living for mankind. As part of this research, nitrogenase of Azotobacter vinelandii was studied to understand the order of events in reduction of substrates and the conformational changes in the enzyme responsible for its ability to reduce said substrates at room temperature and pressure. This knowledge was used to study variant forms of nitrogenase that could be activated using controlled external reductants. This freedom from the biological reductant of nitrogenase opens the door for further research into the understanding and development of enzyme mimics that can reduce substrates at room temperature and pressure.

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Chen, Dawei. "The Methylotrophic Bacterium W3A1 Electron Transfer Flavoprotein: Cloning, Expression, and Cofactor Binding Properties /." The Ohio State University, 1996. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487931993468247.

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Batchelor-McAuley, Christopher. "Multi-electron transfer to and from organic molecules." Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:14f0d2d6-da21-4041-9a5a-e0186fb36239.

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Herein, the influence of protonation and adsorption upon the redox and electrocatalysis of quinone species - specifically anthraquinone derivatives – is investigated. Through the comparison of the measured rate constants of one-electron reductions of a family of quinones in acetonitrile at both graphite and gold electrodes, it was confirmed that the redox potential indirectly influences the rate of electron transfer in a manner consistent with the potential-dependence of the density of states. In aqueous media, the voltammetric response of both anthraquione-2-sulfonate (AQMS) and anthraquinone-2,6-disulfonate (AQDS) was measured over the full aqueous pH range. A model is provided which is able to describe not just the variation in the formal potential but also the peak height as a function of pH. Importantly, this model predicts that the formal potential for the first (Ef1) and second (Ef2) electron transfers are comparable in magnitude (E^θ _f2−E^_θf1 equals -15mV for AQMS and -36mV for AQDS). This quantitative model is then further extended to consider the situation in which the system is not fully buffered, giving insight into the change of pH at the electrode surface during experimentation. Adsorption to graphitic electrodes can impart a strong influence on the measured voltammetric response. It is demonstrated that through the pre-exposure of a newly prepared graphitic electrode to organic solvents, these adsorption processes can be predominantly blocked. Moreover, it is shown that the electroactivity of the electrode is not significantly altered. This thesis also highlights two cases in which adsorption of the electroactive species may be used to positive effect. First, the surface adsorption of anthraquinone-2-monosulfonate is studied on a graphite electrode, where it is demonstrated that the heterogeneity of the electrode surface may be probed through studying the electrochemical response of the adsorbed species. From this work it is concluded that the rate of electron transfer at the graphitic basal plane is 2-3 orders of magnitude lower than that observed on the edge plane sites. Second, the co-adsorption of DNA and anthraquinone-2-monosulfonate is used as an indirect method to measure the solution phase concentration of DNA (LOD = 8.8μM). The reduced form of anthraquinone is also known to readily reduce oxygen. Through the use of a boron-doped diamond electrode it was possible to directly study the anthraquinone mediated reduction mechanism. Significantly, the voltammetric response indicates the reduction of the oxygen via the semi-quinone intermediate (kf = 4.8 × 10⁹ mol⁻¹ dm³ s⁻¹) is over two orders of magnitude faster than the reaction involving the di-reduced form (kf = 1 × 10⁷ mol⁻¹ dm³ s⁻¹). More importantly, this work provides voltammetric evidence for the existence of the semi-quinone species. This work is subsequently extended through the investigation of the poorly soluble anthraquinone derivative quinizarin. Not only is it possible to detect voltammetrically this biologically relevant species to concentrations as low as 5nM (100ppt), but the methodology also allows the electrochemistry of the quinizarin species to be probed, something which was not previously possible.

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Feng, Yucheng. "Role of electrostatic interactions in regulating redox potentials and electron transfer of flavodoxin from Desulfovibrio Vulgaris (Hildenborough)/." The Ohio State University, 1998. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487953204280307.

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Roberts, Lezah Wilette. "Effect of Netropsin on One-electron Oxidation of DNA." Diss., Georgia Institute of Technology, 2005. http://hdl.handle.net/1853/7228.

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One electron oxidation of DNA has been studied extensively over the years. When a charge is injected into a DNA duplex, it migrates through the DNA until it reaches a trap. Upon further reactions, damage occurs in this area and strand cleavage can occur. Many works have been performed to see what can affect this damage to DNA. Netropsin is a minor groove binder that can bind to tracts of four to five A:T base pairs. It has been used in the studies within to determine if it can protect DNA against oxidative damage, caused by one-electron oxidation, when it is bound within the minor groove of the DNA. By using a naphthacenedione derivative as a photosensitizer, several DNA duplexes containing netropsin binding sites as well as those without binding sites, were irradiated at 420 nm, analyzed, and visualized to determine its effect on oxidative damage. It has been determined netropsin creates a quenching sphere of an average of 5.8 * 108 Šwhether bound to the DNA or not. Herein we will show netropsin protects DNA against oxidative damage whether it is free in solutions or bound within the minor groove of a DNA duplex.

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Wallrapp, Frank. "Mixed quantum and classical simulation techniques for mapping electron transfer in proteins." Doctoral thesis, Universitat Pompeu Fabra, 2011. http://hdl.handle.net/10803/22685.

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El objetivo de esta tesis se centra en el estudio de la transferencia de electrones (ET), una de las reacciones más simples y cruciales en bioquímica. Para dichos procesos, obtener información directa de los factores que lo promueves, asi como del camino de transferencia electronica, no es una tarea trivial. Dicha información a un nivel de conocimiento detallado atómico y electrónico, sin embargo, es muy valiosa en términos de una mejor comprensión del ciclo enzimático, que podría conducir, por ejemplo, a un diseño más eficaz de inhibidores. El objetivo principal de esta tesis es el desarrollo de una metodología para el estudio cuantitativo de la ET en los sistemas biológicos. En este sentido, hemos desarrollado un nuevo método para obtener el camino de transferencia electrónico, llamado QM/MM e-‐ Pathway, que se puede aplicar en sistemas complejos con ET de largo alcance. El método se basa en una búsqueda sucesiva de residuos importantes para la ET, utilizando la modificación de la región quantica en métodos mixtos QM/MM, y siguiendo la evolución de la densidad de espín dentro de la zona de transferencia. Hemos demostrado la utilidad y la aplicabilidad del algoritmo en el complejo P450cam/Pdx, identificando el papel clave de la Arg112 (en P450cam) y del Asp48 (en Pdx), ambos conocidos en la literatura. Además de obtener caminos de ET, hemos cuantificado su importancia en términos del acoplamiento electrónico entre el dador y aceptor para los diferentes caminos. En este sentido, se realizaron dos estudios de la influencia del solvente y de la temperatura en el acoplamiento electrónico para sistemas modelo oligopéptidos. Ambos estudios revelaron que los valores del acoplamiento electrónico fluctúan fuertemente a lo largo de las trayectorias de dinámica molecular obtenidas, y el mecanismo de transferencia de electrones se ve ampliamente afectado por el espacio conformacional del sistema. La combinación del QM/MM e-‐pathway y de los cálculos de acoplamiento electronico fueron utilizados finalmente para investigar la ET en el complejo CCP/Cytc. Nuestros hallazgos indican el papel fundamental del Trp191 en localizar un estadio intermedio para la transferencia electronica, así como el camino ET principal que incluye Ala194, Ala193, Gly192 y Trp191. Ambos hallazgos fueron confirmados a través de la literatura. Los resultados obtenidos para el muestro de manios de ET, junto con su evaluación a través de cálculos de acoplamiento electrónico, sugieren un enfoque sencillo y prometedor para investigar ET de largo alcance en proteínas.
The focus of this PhD thesis lies on electron transfer (ET) processes, belonging to the simplest but most crucial reactions in biochemistry. Getting direct information of the forces driving the process and the actual electron pathway is not a trivial task. Such atomic and electronic detailed information, however, is very valuable in terms of a better understanding of the enzymatic cycle, which might lead, for example, to more efficient protein inhibitor design. The main objective of this thesis was the development of a methodology for the quantitative study of ET in biological systems. In this regard, we developed a novel approach to map long-‐range electron transfer pathways, called QM/MM e-‐Pathway. The method is based on a successive search for important ET residues in terms of modifying the QM region following the evolution of the spin density of the electron (hole) within a given transfer region. We proved the usefulness and applicability of the algorithm on the P450cam/Pdx complex, indicating the key role of Arg112 of P450cam and Asp48 of Pdx for its ET pathway, both being known to be important from the literature. Besides only identifying the ET pathways, we further quantified their importance in terms of electronic coupling of donor and acceptor incorporating the particular pathway residues. Within this regard, we performed two systematic evaluations of the underlying reasons for the influence of solvent and temperature onto electronic coupling in oligopeptide model systems. Both studies revealed that electronic coupling values strongly fluctuate throughout the molecular dynamics trajectories obtained, and the mechanism of electron transfer is affected by the conformational space the system is able to occupy. Combining both ET mapping and electronic coupling calculations, we finally investigated the electron transfer in the CcP/Cytc complex. Our findings indicate the key role of Trp191 being the bridge-‐localized state of the ET as well as the main pathway consisting of Ala194, Ala193, Gly192 and Trp191 between CcP and Cytc. Both findings were confirmed through the literature. Moreover, our calculations on several snapshots state a nongated ET mechanism in this protein complex. The methodology developed along this thesis, mapping ET pathways together with their evaluation through electronic coupling calculations, suggests a straightforward and promising approach to investigate long-‐range ET in proteins.

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Abhijit, Saha. "Chemical Biology Approaches for the Molecular Recognition of DNA Double Helix." 京都大学 (Kyoto University), 2015. http://hdl.handle.net/2433/199116.

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Xiong, Ling. "Modification of the protein matrix around active- and inactive pheophytins by site-directed mutagenesis; affects on energy and electron transfer processes in photosystem II /." The Ohio State University, 2002. http://rave.ohiolink.edu/etdc/view?acc_num=osu1486549482671579.

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Ghosh, Avik Kumar. "Charge migration and one-electron oxidation at adenine and thymidine containing DNA strands and role of guanine N1 imino proton in long range charge migration through DNA." Diss., Available online, Georgia Institute of Technology, 2007, 2007. http://etd.gatech.edu/theses/available/etd-05132007-000502/.

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Thesis (Ph. D.)--Chemistry and Biochemistry, Georgia Institute of Technology, 2008.
Wartell, Roger, Committee Member ; Bunz, Uwe, Committee Member ; Doyle, Donald, Committee Member ; Fahrni, Christoph, Committee Member ; Schuster, Gary, Committee Chair.

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Books on the topic "Biology - Electron Transfer"

1

1947-, Bertrand P., ed. Long-range electron transfer in biology. Berlin: Springer-Verlag, 1991.

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S, Bendall D., ed. Protein electron transfer. Oxford, UK: Bios Scientific Publishers, 1996.

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1938-, Müller Achim, ed. Electron and proton transfer in chemistry and biology. Amsterdam: Elsevier, 1992.

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Johnson, Michael K., R. Bruce King, Donald M. Kurtz, Charles Kutal, Michael L. Norton, and Robert A. Scott, eds. Electron Transfer in Biology and the Solid State. Washington, DC: American Chemical Society, 1989. http://dx.doi.org/10.1021/ba-1990-0226.

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1941-, Ulstrup Jens, ed. Electron transfer in chemistry and biology: An introduction to the theory. Chichester: Wiley, 1999.

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Joshua, Jortner, Bixon M, Prigogine I, and Rice Stuart Alan 1932-, eds. Electron transfer- from isolated molecules to biomolecules. New York: J. Wiley, 1999.

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1908-, Gutmann Felix, ed. Charge transfer complexes in biological systems. New York: M. Dekker, 1997.

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1950-, Chakraborty T., ed. Charge migration in DNA: Perspectives from physics, chemistry, and biology. Berlin: Springer, 2007.

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1953-, Johnson Michael K., American Chemical Society. Division of Inorganic Chemistry., and Inorganic Chemistry Symposium (1989 : Athens, Ga.), eds. Electron transfer in biology and the solid state: Inorganic compounds with unusual properties. Washington, DC: American Chemical Society, 1990.

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C, Papageorgiou George, Barber J. 1940-, Papa S, Unesco. European Expert Committee on Biomaterials and Biotechnology. Working Group IV., and Kentron Pyrēnikōn Ereunōn Dēmokritos, eds. Ion interactions in energy transfer biomembranes. New York: Plenum Press, 1986.

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Book chapters on the topic "Biology - Electron Transfer"

1

Rejou-Michel, Agnes, M. Ahsan Habib, and John O’M Bockris. "Electron Transfer at Biological Interfaces." In Electrical Double Layers in Biology, 167–83. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-8145-7_12.

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Williams, R. J. P. "Overview of Biological Electron Transfer." In Electron Transfer in Biology and the Solid State, 3–23. Washington, DC: American Chemical Society, 1989. http://dx.doi.org/10.1021/ba-1990-0226.ch001.

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Morand, Larry Z., R. Holland Cheng, David W. Krogmann, and Kwok Ki Ho. "Soluble Electron Transfer Catalysts of Cyanobacteria." In The Molecular Biology of Cyanobacteria, 381–407. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0227-8_12.

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Therien, Michael J., Jeffrey Chang, Adrienne L. Raphael, Bruce E. Bowler, and Harry B. Gray. "Long-range electron transfer in metalloproteins." In Long-Range Electron Transfer in Biology, 109–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/3-540-53260-9_4.

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Siedow, James N. "Bioenergetics: The Mitochondrial Electron Transfer Chain." In The molecular biology of plant mitochondria, 281–312. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0163-9_8.

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Barrows, Julie N., and Michael T. Pope. "Intramolecular Electron Transfer and Electron Delocalization in Molybdophosphate Heteropoly Anions." In Electron Transfer in Biology and the Solid State, 403–17. Washington, DC: American Chemical Society, 1989. http://dx.doi.org/10.1021/ba-1990-0226.ch021.

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Cammack, Richard, and Fraser MacMillan. "Electron Magnetic Resonance of Iron–Sulfur Proteins in Electron-Transfer Chains: Resolving Complexity." In Metals in Biology, 11–44. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1139-1_2.

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Cabana, Leonardo A., and Kirk S. Schanze. "Photoinduced Electron Transfer Across Peptide Spacers." In Electron Transfer in Biology and the Solid State, 101–24. Washington, DC: American Chemical Society, 1989. http://dx.doi.org/10.1021/ba-1990-0226.ch005.

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Bertrand, Patrick. "Application of electron transfer theories to biological systems." In Long-Range Electron Transfer in Biology, 1–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/3-540-53260-9_1.

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Kuki, Atsuo. "Electronic tunneling paths in proteins." In Long-Range Electron Transfer in Biology, 49–83. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/3-540-53260-9_2.

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Conference papers on the topic "Biology - Electron Transfer"

1

Yoshihara, Keitaro, Haridas Pal, Hideaki Shirota, Yutaka Nagasawa, and Keisuke Tominaga. "Ultrafast Dynamics in Intermolecular Electron Transfer." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1996. http://dx.doi.org/10.1364/up.1996.tha.6.

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Electron Transfer (ET) is one of the most common reactions in chemistry and biology. For the past decade critical comparison between theory1,2 and experiments3-6 has been giving important insight into the dynamical aspects of ET in solution. Contemporary ET theories which are based only upon the solvent polarization relaxation have predicted that the ET reactions are controlled by the solvent fluctuations and the maximum ET rate for a barriers reaction cannot exceed the solvation rates. The dependence of the ET rate constants on the solvation times has experimentally been demonstrated by many authors.

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OLIVEIRA, M. A., and W. J. BAADER. "EFFICIENCY OF ELECTRON-TRANSFER INDUCED CHEMIEXCITATION: A COMPARISON OF INTER- AND INTRAMOLECULAR PROCESSES." In Chemistry, Biology and Applications. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812770196_0056.

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Komirisetty, Archana, Frances Williams, Aswini Pradhan, and Meric Arslan. "Integrating Sensors With Nanostructures for Biomedical Applications." In ASME 2013 2nd Global Congress on NanoEngineering for Medicine and Biology. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/nemb2013-93121.

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This paper presents the fabrication of sensors that are integrated with nanostructures and bio-functionalized to create novel devices for biomedical applications. Biosensors are in great demand for various applications including for the agriculture and food industries, environmental monitoring, and medical diagnostics. Much research is being focused on the use of nanostructures (nanowires, nanotubes, nanoparticles, etc.) to provide for miniaturization and improved performance of these devices. The use of nanostructures is favorable for such applications since their sizes are closer to that of biological and chemical species and therefore, improve the signal generated. Moreover, their high surface-to-volume ratio results in devices with very high sensitivity. The use of nanotechnology leads to smaller, lower-power smart devices. Thus, this paper presents the integration of sensors with nanostructures for biomedical applications, specifically, glucose sensing. In the work presented, a glucose biosensor and its fabrication process flow are described. The device is based on electrochemical sensing using a working electrode with bio-functionalized zinc oxide (ZnO) nano-rods. Among all metal oxide nanostructures, ZnO nano-materials play a significant role as a sensing element in biosensors due to their properties such as high isoelectric point (IEP), fast electron transfer, non-toxicity, biocompatibility, and chemical stability which are very crucial parameters to achieve high sensitivity. Amperometric enzyme electrodes based on glucose oxidase (GOx) are used due to their stability and high selectivity to glucose. The device also consists of silicon dioxide and titanium layers as well as platinum working and counter electrodes and a silver/silver chloride reference electrode. The chlorination process on the reference electrode was optimized for various times using field emission scanning electron microscope (FESEM) and energy-dispersive X-ray spectroscopy (EDS or EDX) measurements. The ZnO nanorods were grown using the hydrothermal method and will be bio-functionalized with GOx for electrochemical sensing. Once completed, the sensors will be tested to characterize their performance, including their sensitivity and stability.

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Drzewiecki, G., H. Katta, Andreas Pfahnl, David Bello, and David Dicken. "Active and passive stethoscope frequency transfer functions: Electronic stethoscope frequency response." In 2014 IEEE Signal Processing in Medicine and Biology Symposium (SPMB). IEEE, 2014. http://dx.doi.org/10.1109/spmb.2014.7002962.

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Korshunova, A. N., and V. D. Lakhno. "Various regimes of charge transfer in a Holstein chain in a constant electric field depending on its intensity and the initial charge distribution." In Mathematical Biology and Bioinformatics. Pushchino: IMPB RAS - Branch of KIAM RAS, 2018. http://dx.doi.org/10.17537/icmbb18.89.

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Hackworth, S. A., Mingui Sun, and R. J. Sclabassi. "Skin-electrode circuit model for use in optimizing energy transfer in volume conduction systems." In 2009 Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2009. http://dx.doi.org/10.1109/iembs.2009.5334112.

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Chen, Zhaoyang, Hongwei Hao, Luming Li, and Jie Dong. "Wavelet Transform for Rabbit EEG with Vagus Nerve Electric Stimulation." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.260698.

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Chen, Zhaoyang, Hongwei Hao, Luming Li, and Jie Dong. "Wavelet Transform for Rabbit EEG with Vagus Nerve Electric Stimulation." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.4397753.

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Datta, A., M. Elwassif, and M. Bikson. "Bio-heat transfer model of transcranial DC stimulation: Comparison of conventional pad versus ring electrode." In 2009 Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2009. http://dx.doi.org/10.1109/iembs.2009.5333673.

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Yu Zhao, M. Nandra, Chia-Chen Yu, and Yu-chong Tai. "High performance 3-coil wireless power transfer system for the 512-electrode epiretinal prosthesis." In 2012 34th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2012. http://dx.doi.org/10.1109/embc.2012.6347503.

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