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Results: 1-9 |
Results: 9
Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus
Authors: Logan, C Mayhew, SG
Citation: C. Logan et Sg. Mayhew, Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus, J BIOL CHEM, 275(39), 2000, pp. 30019-30028
Cloning, sequencing and expression of the gene for flavodoxin from Megasphaera elsdenii and the effects of removing the protein negative charge that is closest to N(1) of the bound FMN
Authors: Geoghegan, SM Mayhew, SG Yalloway, GN Butler, G
Citation: Sm. Geoghegan et al., Cloning, sequencing and expression of the gene for flavodoxin from Megasphaera elsdenii and the effects of removing the protein negative charge that is closest to N(1) of the bound FMN, EUR J BIOCH, 267(14), 2000, pp. 4434-4444
Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp, strain OxB-1: Purification, characterization, and molecular cloning of the gene
Authors: Kato, Y Nakamura, K Sakiyama, H Mayhew, SG Asano, Y
Citation: Y. Kato et al., Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp, strain OxB-1: Purification, characterization, and molecular cloning of the gene, BIOCHEM, 39(4), 2000, pp. 800-809
Detection of scalar couplings across NH center dot center dot center dot OP and OH center dot center dot center dot OP hydrogen bonds in a flavoprotein
Authors: Lohr, F Mayhew, SG Ruterjans, H
Citation: F. Lohr et al., Detection of scalar couplings across NH center dot center dot center dot OP and OH center dot center dot center dot OP hydrogen bonds in a flavoprotein, J AM CHEM S, 122(38), 2000, pp. 9289-9295
Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1
Authors: Mac Sweeney, A D'Arcy, A Higgins, TM Mayhew, SG Toomey, D Walsh, MA
Citation: A. Mac Sweeney et al., Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1, ACT CRYST D, 55, 1999, pp. 297-298
The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide - A reappraisal
Authors: Mayhew, SG
Citation: Sg. Mayhew, The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide - A reappraisal, EUR J BIOCH, 265(2), 1999, pp. 698-702
pH-Dependent spectroscopic changes associated with the hydroquinone of FMNin flavodoxins
Authors: Yalloway, GN Mayhew, SG Malthouse, JPG Gallagher, ME Curley, GP
Citation: Gn. Yalloway et al., pH-Dependent spectroscopic changes associated with the hydroquinone of FMNin flavodoxins, BIOCHEM, 38(12), 1999, pp. 3753-3762
Potentiometric measurement of oxidation-reduction potentials
Authors: Mayhew, SG
Citation: Sg. Mayhew, Potentiometric measurement of oxidation-reduction potentials, METH MOL B, 131, 1999, pp. 49-59
X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough) apoflavodoxin-riboflavin complex
Authors: Walsh, MA McCarthy, A O'Farrell, PA McArdle, P Cunningham, PD Mayhew, SG Higgins, TM
Citation: Ma. Walsh et al., X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough) apoflavodoxin-riboflavin complex, EUR J BIOCH, 258(2), 1998, pp. 362-371
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