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Your search keyword '"Yalloway, Gary N."' showing total 3 results
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3 results on '"Yalloway, Gary N."'

1. Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin

Author

McCarthy, Andrew A., Walsh, Martin A., Verma, Chandra S., O'Connell, David P., Reinhold, Meike, Yalloway, Gary N., d'Arcy, Darren, Higgins, Timothy M., Voordouw, Gerrit, and Mayhew, Stephen G.

Subjects
Proteins -- Electric properties, Amino acids -- Structure-activity relationships, Membrane potentials -- Physiological aspects, Structure-activity relationships (Biochemistry) -- Analysis, Biological sciences, Chemistry
Abstract

Structural and charge interaction analyses of the binding site of the aspartate 95 mutants of the Desulfovibrio vulgaris flavodoxin reveals the role played by the hydrogen bonding in the modulation of the redox potentials of the bound flavodoxin, particularly the carboxylate group of the mutant.

Published
2002

2. Kinetic stability of the flavin semiquinone in photolyase and cryptochrome-DASH

Author

Damiani, Michael J., Yalloway, Gary N., Lu, Jessica, McLeod, Neahlanna R., and O'Neill, Melanie A.

Subjects
Cytochromes -- Chemical properties, Cytochromes -- Structure, DNA repair -- Analysis, Electron transport -- Analysis, Bioflavonoids -- Chemical properties, Bioflavonoids -- Structure, Flavones -- Chemical properties, Flavones -- Structure, Flavonoids -- Chemical properties, Flavonoids -- Structure, Photolysis -- Analysis, Biological sciences, Chemistry
Abstract

A study was conducted to understand the kinetic mechanism related to the role of structurally homologous flavoproteins photolyases and cryptochromes (CRY) towards UV-damaged DNA repair by photoinduced electron transfer from their FAD cofactor. The results obtained offer insight into the kinetic tuning of the rates of electron transfer which would play a function-defining role in photolyases and cryptochromes.

Published
2009

3. pH-dependent spectroscopic changes associated with the hydroquinone of FMN in flavodoxins

Author

Yalloway, Gary N., Mayhew, Stephen G., Malthouse, J. Paul G., Gallagher, Mary E., and Curley, G. Paul

Subjects
Hydroquinone -- Research, Hydrogen-ion concentration -- Research, Hydrogen bonding -- Research, Proteins -- Research, Biological sciences, Chemistry
Abstract

A study was conducted to analyze pH-dependent spectroscopic changes related to the hydroquinone of FMN in flavodoxins. Flavodoxin from D. vulgaris was determined as the recombinant protein. Results indicated that a decrease in pH promotes a change in the electronic structure of the reduced flavin resulting from changes in the ionization state of the flavin and in the hydrogen-bonding network around the flavin.

Published
1999

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