Evidence for the presence of the reductive pentose phosphate cycle in a filamentous anoxygenic photosynthetic bacterium, Oscillochloris trichoides strain DG-6
1 Department of Microbiology, Moscow State University, Moscow, 119899, Russia 2 Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, 142292, Russia Author for correspondence: Ruslan N. Ivanovsky. Tel: -7 095 939 4203. Fax: -7 095 939 4658. e-mail: rusla...
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Published in: | Microbiology (Society for General Microbiology) Vol. 145; no. 7; pp. 1743 - 1748 |
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Main Authors: | , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
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Soc General Microbiol
01-07-1999
Society for General Microbiology |
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Summary: | 1 Department of Microbiology, Moscow State University, Moscow, 119899, Russia
2 Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, 142292, Russia
Author for correspondence: Ruslan N. Ivanovsky. Tel: -7 095 939 4203. Fax: -7 095 939 4658. e-mail: ruslan@protein.bio.msu.su
ABSTRACT
Studies on autotrophic CO 2 fixation by the filamentous anoxygenic photosynthetic bacterium Oscillochloris trichoides strain DG-6 demonstrated that, unlike other green bacteria, this organism metabolized CO 2 via the reductive pentose phosphate cycle. Both key enzymes of this cycle — ribulose-1,5-bisphosphate carboxylase/oxygenase and phosphoribulokinase — were detected in cell extracts. The main product of ribulose 1,5-bisphosphate-dependent CO 2 fixation was 3-phosphoglyceric acid. KCN, which is known to be a competitive inhibitor of ribulose-1,5-bisphosphate carboxylase/oxygenase, completely in hibited the CO 2 assimilation by whole cells as well as by cell extracts of O. trichoides. The 13 C/ 12 C carbon isotope fractionation during photoautotrophic growth of O. trichoides was -19·7°/ , which is close to that obtained for autotrophic organisms that use ribulose-1,5-bisphosphate carboxylase as the primary carboxylation enzyme. Cell extracts of O. trichoides contained all the enzymes of the tricarboxylic acid cycle except 2-oxoglutarate dehydrogenase. No activity of isocitrate lyase, a key enzyme of the glyoxylate shunt, was found in cell extracts of O. trichoides DG-6.
Keywords: green bacteria, Oscillochloris trichoides, CO 2 fixation pathway, ribulose-1,5-bisphosphate carboxylase/oxygenase, tricarboxylic acid cycle |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1350-0872 1465-2080 |
DOI: | 10.1099/13500872-145-7-1743 |