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MOLECULAR COMPLEXES OF FLAVINS AND PHENOLSFleischman, Darrell Eugene, 1934- January 1965 (has links)
No description available.
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Characterization of the iron center in cysteine dioxygenase and kinetic analyses of flavin binding by the alkanesulfonate flavin reductaseSun, Honglei, Ellis, Holly R. January 2006 (has links) (PDF)
Thesis(M.S.)--Auburn University, 2006. / Abstract. Vita. Includes bibliographic references (p.90-94).
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TRANSIENT KINETICS OF ELECTRON TRANSFER REACTIONS OF FLAVODOXIN (CLOSTRIDIUM, PASTEURIANUM).SIMONDSEN, ROYCE PAUL. January 1983 (has links)
Electron transfer reactions between Clostridium pasteurianum flavodoxin semiquinone and various oxidants (horse heart cytochrome c, ferricyanide, and ferric EDTA) have been studied as a function of ionic strength using stopped-flow spectrophotometry. The cytochrome c reaction is complicated by the existence of two cytochrome species which react at different rates and whose relative concentrations are ionic strength dependent. Only the faster of these two reactions is considered here. At low ionic strength, complex formation between cytochrome c and flavodoxin is indicated by a levelling-off of the pseudo-first order rate constant at high cytochrome c concentration. This is not observed for either ferricyanide or ferric EDTA. For cytochrome c, the rate and association constants for complex formation were found to increase with decreasing ionic strength, consistent with negative charges on flavodoxin interacting with the positively charged cytochrome electron transfer site. Both ferricyanide and ferric EDTA are negatively charged oxidants and the rate data respond to ionic strength changes as would be predicted for reactants of the same charge sign. These results demonstrate that electrostatic interactions involving negatively charged groups are important in orienting flavodoxin with respect to oxidants during electron transfer. The effects of structural modifications of the FMN prosthetic group of C. pasteurianum flavodoxin on the kinetics of electron transfer to the oxidized form (from 5-deazariboflavin semiquinone produced by laser flash photolysis) and from the semiquinone form (to horse heart cytochrome c using stopped-flow spectrophotometry) have been investigated. The analogs used were 7,8-dichloroFMN, 8-chloroFMN, 7-chloroFMN and 5,6,7,8-tetrahydroFMN. The ionic strength dependence of cytochrome c reduction was not affected by chlorine substitution, although the specific rate constants for complex formation and decay were appreciably smaller. On the other hand, all of the chlorine analogs had the same rate constant for deazariboflavin semiquinone oxidation. The rate constants for tetrahydroFMN flavodoxin semiquinone reduction of cytochrome c were considerably smaller than those for the native protein. The results for the chlorine analogs indicate the important roles that the polarity of the exposed flavin edge and the substitution of the 8 position play in electron transfer. The data obtained with the tetrahydroFMN analog indicates that the (pi) electron system of the flavin is necessary for rapid electron transfer. These implications are discussed for the electron transfer mechanism of flavodoxin.
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Study of two proteins involved in protein disulphide formation molecular cloning and characterization of a full-length flavin-dependent monooxygenase from Saccharomyces cerevisiae & preliminary structure analysis on DsbC from Haemophilus influenzae /Zhang, Man, January 2003 (has links)
Thesis (Ph. D.)--University of Texas at Austin, 2003. / Vita. Includes bibliographical references. Available also from UMI Company.
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Study of two proteins involved in protein disulphide formation : molecular cloning and characterization of a full-length flavin-dependent monooxygenase from Saccharomyces cerevisiae & preliminary structure analysis on DsbC from Haemophilus influenzaeZhang, Man, 1972- 27 July 2011 (has links)
Not available / text
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The mechanisms of flavin site reactions in NADH:ubiquinone oxidoreductaseBirrell, James Alexander January 2013 (has links)
No description available.
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Functional roles of conserved active site amino acids in the desulfonation reaction catalyzed by the alkanesulfonate monooxygenase from Escheria coliCarpenter, Russell, Ellis, Holly R., January 2008 (has links)
Thesis (Ph. D.)--Auburn University. / Abstract. Vita. Includes bibliographical references (p. 156-168).
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Catalytic mechanism of a flavin-dependent alkanesulfonate monoxygenase from Escherichia coliZhan, Xuanzhi, Ellis, Holly R., January 2008 (has links) (PDF)
Thesis (Ph. D.)--Auburn University, 2008. / Abstract. Vita. Includes bibliographical references (p. 154-166).
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Separation of endogenous fluorophores in normal and cancer cellsLi, Ye. Geng, M. Lei. January 2009 (has links)
Thesis supervisor: M. Lei Geng. Includes bibliographic references (p. 203-217).
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The chemistry of flavins and related systemsHiggins, Raymond January 1965 (has links)
No description available.
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