Characterization of hydrogenosomes and their role in glucose metabolism of Neocallimastix sp. L2 |
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Authors: | Femke D. Marvin-Sikkema Teresa M. Pedro Gomes Jean-Philippe Grivet Jan C. Gottschal Rudolf A. Prins |
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Affiliation: | (1) Department of Microbiology, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands;(2) Centre de Biophysique Moleculaire, CNRS, 1A Avenue de la Recherche Scientifique, F-45071 Orléans Cedex 2, France;(3) Present address: Division of Industrial Microbiology, Department of Food Science, Wageningen Agricultural University, P.O. Box 8129, 6700 EV Wageningen, The Netherlands |
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Abstract: | In the anaerobic fungus Neocallimastix sp. L2 fermentation of glucose proceeds via the Embden-Meyerhof-Parnas pathway. Enzyme activities leading to the formation of succinate, lactate, ethanol, and formate are associated with the cytoplasmic fraction. The enzymes malic enzyme, NAD(P)H: ferredoxin oxidoreductase, pyruvate: ferredoxin oxidoreductase, hydrogenase, acetate: succinate CoA transferase and succinate thiokinase leading to the formation of H2, CO2, acetate, and ATP are localized in microbodies. Thus, these organelles are identified as hydrogenosomes. In addition, the microbodies contain the O2-scavenging enzymes NADH- and NADPH oxidase, while NAD(P)H peroxidase, catalase, or superoxide dismutase could not be detected. In cell-free extracts from zoospores of Neocallimastix sp. L2 the specific activities of hydrogenosomal enzymes as well as the quantities of these proteins are 2- to 6-fold higher than in mycelium extracts. These findings suggest that hydrogenosomes perform an important role-especially in zoospores — as H2-evolving, ATP-generating and O2-scavenging organelles.Abbrevations DTT Dithiotreitol - PEP Phosphoenol pyruvate |
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Keywords: | Anaerobic fungus Neocallimastix Glucose metabolism Hydrogenosomes |
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