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S Ghisla

Showing results (31-40 of 104) with videos related to

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Biochemistry|September 9, 2000
Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarumK Tittmann, R Golbik, S Ghisla, et al.
The Journal of Biological Chemistry|November 10, 1984
4-Thioflavins as active site probes of flavoproteins. Reactions with sulfiteM Biemann, A Claiborne, S Ghisla, et al.
The Journal of Biological Chemistry|August 10, 1984
4-Thioflavins as active site probes of flavoproteins. General propertiesV Massey, A Claiborne, M Biemann, et al.
European Journal of Biochemistry|July 1, 1991
Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analoguesU Ermler, S Ghisla, V Massey, et al.
The Journal of Biological Chemistry|October 18, 1996
Studies with flavin analogs provide evidence that a protonated reduced FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthaseP Macheroux, S Bornemann, S Ghisla, et al.
European Journal of Biochemistry|April 15, 1985
FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structureR L Krauth-Siegel, R H Schirmer, S Ghisla
European Journal of Biochemistry|May 1, 1989
Bioluminescence emission of bacterial luciferase with 1-deaza-FMN. Evidence for the noninvolvement of N(1)-protonated flavin species as emittersM Kurfürst, P Macheroux, S Ghisla, et al.
The Journal of Biological Chemistry|June 9, 2001
Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pairR Coulombe, K Q Yue, S Ghisla, et al.
European Journal of Biochemistry|April 1, 1982
Structure and catalytic inactivity of the bacterial luciferase neutral flavin radicalM Kurfürst, S Ghisla, R Presswood, et al.
Biochemistry|August 23, 1988
Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple. A new investigation of the rapid reaction kineticsL M Schopfer, V Massey, S Ghisla, et al.
Pageof 11

Showing results (31-40 of 104) with videos related to

Sort By:
Pageof 11
Biochemistry|September 9, 2000
Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarumK Tittmann, R Golbik, S Ghisla, et al.
The Journal of Biological Chemistry|November 10, 1984
4-Thioflavins as active site probes of flavoproteins. Reactions with sulfiteM Biemann, A Claiborne, S Ghisla, et al.
The Journal of Biological Chemistry|August 10, 1984
4-Thioflavins as active site probes of flavoproteins. General propertiesV Massey, A Claiborne, M Biemann, et al.
European Journal of Biochemistry|July 1, 1991
Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analoguesU Ermler, S Ghisla, V Massey, et al.
The Journal of Biological Chemistry|October 18, 1996
Studies with flavin analogs provide evidence that a protonated reduced FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthaseP Macheroux, S Bornemann, S Ghisla, et al.
European Journal of Biochemistry|April 15, 1985
FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structureR L Krauth-Siegel, R H Schirmer, S Ghisla
European Journal of Biochemistry|May 1, 1989
Bioluminescence emission of bacterial luciferase with 1-deaza-FMN. Evidence for the noninvolvement of N(1)-protonated flavin species as emittersM Kurfürst, P Macheroux, S Ghisla, et al.
The Journal of Biological Chemistry|June 9, 2001
Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pairR Coulombe, K Q Yue, S Ghisla, et al.
European Journal of Biochemistry|April 1, 1982
Structure and catalytic inactivity of the bacterial luciferase neutral flavin radicalM Kurfürst, S Ghisla, R Presswood, et al.
Biochemistry|August 23, 1988
Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple. A new investigation of the rapid reaction kineticsL M Schopfer, V Massey, S Ghisla, et al.
Pageof 11