L
Laurence Girbal
Researcher at University of Toulouse
Publications - 48
Citations - 2810
Laurence Girbal is an academic researcher from University of Toulouse. The author has contributed to research in topics: Clostridium acetobutylicum & Gene expression. The author has an hindex of 26, co-authored 43 publications receiving 2633 citations. Previous affiliations of Laurence Girbal include Institut national des sciences appliquées de Toulouse & University of Georgia.
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Journal ArticleDOI
Regulation of carbon and electron flow in Clostridium acetobutylicum grown in chemostat culture at neutral pH on mixtures of glucose and glycerol.
TL;DR: The metabolism of Clostridium acetobutylicum was manipulated, at neutral pH and in chemostat culture, by changing the overall degree of reduction of the substrate, using mixtures of glucose and glycerol to indicate the absence of butyraldehyde dehydrogenase activity and very low levels of coenzyme A-transferase, butanol, and ethanol dehydrogenases.
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Molecular Characterization and Transcriptional Analysis of adhE2, the Gene Encoding the NADH-Dependent Aldehyde/Alcohol Dehydrogenase Responsible for Butanol Production in Alcohologenic Cultures of Clostridium acetobutylicum ATCC 824
Lisa Fontaine,Isabelle Meynial-Salles,Laurence Girbal,Xinghong Yang,Christian Croux,Philippe Soucaille,Philippe Soucaille +6 more
TL;DR: The adhE2 gene of Clostridium acetobutylicum ATCC 824, coding for an aldehyde/alcohol dehydrogenase (AADH), was characterized from molecular and biochemical points of view and is the first example of a bacterium with two AADHs.
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Regulation of carbon and electron flow in Clostridium butyricum VPI 3266 grown on glucose-glycerol mixtures.
TL;DR: The metabolism of Clostridium butyricum was manipulated at pH 6.5 and in phosphate-limited chemostat culture by changing the overall degree of reduction of the substrate using mixtures of glucose and glycerol to show changes in acetate and butyrate formation and the stoichiometry of the H(+) ATPase was shown to remain constant.
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Insight into the mechanism of the B12-independent glycerol dehydratase from Clostridium butyricum: preliminary biochemical and structural characterization.
Jessica R. O’Brien,Céline Raynaud,Christian Croux,Laurence Girbal,Philippe Soucaille,William N. Lanzilotta +5 more
TL;DR: The molecular characterization of a B12-independent glycerol dehydratase from Clostridium butyricum has been reported, and a mechanism for the dehydration reaction clearly supports a concerted pathway for migration of the OH group through a cyclic transition state that is stabilized by partial protonation of the migrating OH group.
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Regulation of metabolic shifts in Clostridium acetobutylicum ATCC 824
TL;DR: In this paper, the authors showed that a high NADH level leading to butanol and ethanol formation was accompanied by increased activities of the NADH-dependent alcohol and butyraldehyde dehydrogenases, and ferredoxin:NAD(P) + reductases.