18 results on '"Soucaille, Philippe"'
Search Results
2. Electrochemical Measurements of the Kinetics of Inhibition of Two FeFe Hydrogenases by O2 Demonstrate That the Reaction Is Partly Reversible.
3. Correction to “Steady-State Catalytic Wave-Shapes for 2-Electron Reversible Electrocatalysts and Enzymes”
4. Mechanism of O2diffusion and reduction in FeFe hydrogenases
5. Steady-State Catalytic Wave-Shapes for 2-Electron Reversible Electrocatalysts and Enzymes.
6. Covalent Attachment of FeFe Hydrogenases to Carbon Electrodes for Direct Electron Transfer.
7. CO Disrupts the Reduced H-Cluster of FeFe Hydrogenase. A Combined DFT and Protein Film Voltammetry Study.
8. Insight into the Mechanism of the B12-Independent Glycerol Dehydratase from Clostridium butyricum: Preliminary Biochemical and Structural Characterization.
9. Comparative Genomic Analysis of dhaRegulon and Related Genes for Anaerobic Glycerol Metabolism in Bacteria
10. Transcript Quantification Based on Chemical Labeling of RNA Associated with Fluorescent Detection
11. Effects of various alcoholic supplements on the growth rate of Clostridium acetobutylicum ATCC 824
12. A tentative physiological model of batch acetonobutylic fermentation
13. Butanol tolerance and autobacteriocin production byClostridium acetobutylicum
14. Acetonobutylic fermentation byClostridium acetobutylicum ATCC 824: Autobacteriocin production, properties, and effects
15. Uncoupled glycerol distribution as the origin of the accumulation of 3-hydroxypropionaldehyde during the fermentation of glycerol by <TOGGLE>Enterobacter agglomerans</TOGGLE> CNCM 1210
16. Author Correction: The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster
17. Cap0037, a Novel Global Regulator of Clostridium acetobutylicumMetabolism
18. A Quantitative System-Scale Characterization of the Metabolism of Clostridium acetobutylicum
Catalog
Books, media, physical & digital resources
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.