Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium
Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A.
American Association for the Advancement of Science (AAAS)
Published 2018
American Association for the Advancement of Science (AAAS)
Published 2018
| Publication Date: |
2018-02-03
|
|---|---|
| Publisher: |
American Association for the Advancement of Science (AAAS)
|
| Print ISSN: |
0036-8075
|
| Electronic ISSN: |
1095-9203
|
| Topics: |
Biology
Chemistry and Pharmacology
Geosciences
Computer Science
Medicine
Natural Sciences in General
Physics
|
| Keywords: |
Biochemistry, Microbiology
|
| Published by: |
| _version_ | 1836398776755945472 |
|---|---|
| autor | Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. |
| beschreibung | Biological inorganic carbon fixation proceeds through a number of fundamentally different autotrophic pathways that are defined by specific key enzymatic reactions. Detection of the enzymatic genes in (meta)genomes is widely used to estimate the contribution of individual organisms or communities to primary production. Here we show that the sulfur-reducing anaerobic deltaproteobacterium Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate independently into acetyl coenzyme A and oxaloacetate, a reaction that has been regarded as impossible under physiological conditions. Because this overlooked, energetically efficient carbon fixation pathway lacks key enzymes, it may function unnoticed in many organisms, making bioinformatical predictions difficult, if not impossible. |
| citation_standardnr | 6154428 |
| datenlieferant | ipn_articles |
| feed_id | 25 |
| feed_publisher | American Association for the Advancement of Science (AAAS) |
| feed_publisher_url | http://www.aaas.org/ |
| insertion_date | 2018-02-03 |
| journaleissn | 1095-9203 |
| journalissn | 0036-8075 |
| publikationsjahr_anzeige | 2018 |
| publikationsjahr_facette | 2018 |
| publikationsjahr_intervall | 7984:2015-2019 |
| publikationsjahr_sort | 2018 |
| publisher | American Association for the Advancement of Science (AAAS) |
| quelle | Science |
| relation | http://science.sciencemag.org/cgi/content/short/359/6375/563?rss=1 |
| schlagwort | Biochemistry, Microbiology |
| search_space | articles |
| shingle_author_1 | Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. |
| shingle_author_2 | Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. |
| shingle_author_3 | Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. |
| shingle_author_4 | Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. |
| shingle_catch_all_1 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium Biochemistry, Microbiology Biological inorganic carbon fixation proceeds through a number of fundamentally different autotrophic pathways that are defined by specific key enzymatic reactions. Detection of the enzymatic genes in (meta)genomes is widely used to estimate the contribution of individual organisms or communities to primary production. Here we show that the sulfur-reducing anaerobic deltaproteobacterium Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate independently into acetyl coenzyme A and oxaloacetate, a reaction that has been regarded as impossible under physiological conditions. Because this overlooked, energetically efficient carbon fixation pathway lacks key enzymes, it may function unnoticed in many organisms, making bioinformatical predictions difficult, if not impossible. Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_2 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium Biochemistry, Microbiology Biological inorganic carbon fixation proceeds through a number of fundamentally different autotrophic pathways that are defined by specific key enzymatic reactions. Detection of the enzymatic genes in (meta)genomes is widely used to estimate the contribution of individual organisms or communities to primary production. Here we show that the sulfur-reducing anaerobic deltaproteobacterium Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate independently into acetyl coenzyme A and oxaloacetate, a reaction that has been regarded as impossible under physiological conditions. Because this overlooked, energetically efficient carbon fixation pathway lacks key enzymes, it may function unnoticed in many organisms, making bioinformatical predictions difficult, if not impossible. Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_3 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium Biochemistry, Microbiology Biological inorganic carbon fixation proceeds through a number of fundamentally different autotrophic pathways that are defined by specific key enzymatic reactions. Detection of the enzymatic genes in (meta)genomes is widely used to estimate the contribution of individual organisms or communities to primary production. Here we show that the sulfur-reducing anaerobic deltaproteobacterium Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate independently into acetyl coenzyme A and oxaloacetate, a reaction that has been regarded as impossible under physiological conditions. Because this overlooked, energetically efficient carbon fixation pathway lacks key enzymes, it may function unnoticed in many organisms, making bioinformatical predictions difficult, if not impossible. Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_4 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium Biochemistry, Microbiology Biological inorganic carbon fixation proceeds through a number of fundamentally different autotrophic pathways that are defined by specific key enzymatic reactions. Detection of the enzymatic genes in (meta)genomes is widely used to estimate the contribution of individual organisms or communities to primary production. Here we show that the sulfur-reducing anaerobic deltaproteobacterium Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate independently into acetyl coenzyme A and oxaloacetate, a reaction that has been regarded as impossible under physiological conditions. Because this overlooked, energetically efficient carbon fixation pathway lacks key enzymes, it may function unnoticed in many organisms, making bioinformatical predictions difficult, if not impossible. Mall, A., Sobotta, J., Huber, C., Tschirner, C., Kowarschik, S., Bacnik, K., Mergelsberg, M., Boll, M., Hügler, M., Eisenreich, W., Berg, I. A. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_title_1 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium |
| shingle_title_2 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium |
| shingle_title_3 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium |
| shingle_title_4 | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium |
| timestamp | 2025-06-30T23:32:27.978Z |
| titel | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium |
| titel_suche | Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium |
| topic | W V TE-TZ SQ-SU WW-YZ TA-TD U |
| uid | ipn_articles_6154428 |