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Biological electron transfer
- Date Issued:
- 2008
- Summary:
- Most living organisms utilize electron transport chains in order to obtain energy. Riboflavin, commonly known as vitamin B2, is the central component of the redox coenzymes flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). These cofactors serve as a prosthetic group to flavoproteins and function as the energy-carrying molecules in electron transfer reactions. In this study, the different ionization and oxidation states of riboflavin were identified and quantified as a function of solution potential and pH. To accomplish this task, spectroelectrochemical reductions of riboflavin at different pH were performed. Spectroscopic data offer clues concerning the identity of underlying species, such as oxidation/ionization states and the controlling equilibria. The large data sets obtained from these experiments were analyzed and the acid dissociation constant for reduced riboflavin was determined.
Title: | Biological electron transfer: an investigation of riboflavin. |
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Name(s): |
Caplan, Stacee Lee Harriet L. Wilkes Honors College |
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Type of Resource: | text | |
Genre: | Thesis | |
Issuance: | multipart monograph | |
Date Issued: | 2008 | |
Publisher: | Florida Atlantic University | |
Physical Form: |
electronic electronic resource |
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Extent: | vii, 13 leaves : ill. | |
Language(s): | English | |
Summary: | Most living organisms utilize electron transport chains in order to obtain energy. Riboflavin, commonly known as vitamin B2, is the central component of the redox coenzymes flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). These cofactors serve as a prosthetic group to flavoproteins and function as the energy-carrying molecules in electron transfer reactions. In this study, the different ionization and oxidation states of riboflavin were identified and quantified as a function of solution potential and pH. To accomplish this task, spectroelectrochemical reductions of riboflavin at different pH were performed. Spectroscopic data offer clues concerning the identity of underlying species, such as oxidation/ionization states and the controlling equilibria. The large data sets obtained from these experiments were analyzed and the acid dissociation constant for reduced riboflavin was determined. | |
Identifier: | 299780739 (oclc), 77660 (digitool), FADT77660 (IID), fau:1480 (fedora) | |
Note(s): |
by Stacee Caplan. Thesis (B.A.)--Florida Atlantic University, Honors College, 2008. Bibliography: leaf 13. Electronic reproduction. Boca Raton, Fla., 2008. Mode of access: World Wide Web. |
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Subject(s): |
Solution (Chemistry) Electron spectroscopy Chemical reaction, Conditions and laws of Charge transfer in biology |
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Held by: | FBoU FAUER | |
Persistent Link to This Record: | http://purl.flvc.org/FAU/77660 | |
Use and Reproduction: | Copyright © is held by the author, with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder. | |
Host Institution: | FAU |