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Purification, some properties and quaternary structure of the d -ribulose 1,5-diphosphate carboxylase of Alcaligenes eutrophus

Purification, some properties and quaternary structure of the d -ribulose 1,5-diphosphate... 203 110 110 2 3 B. Bowien F. Mayer G. A. Codd H. G. Schlegel Institut für Mikrobiologie der Universität Grisebachstr. 8 D-3400 Göttingen Federal Republic of Germany der Gesellschaft für Strahlen-und Umweltforschung mbH Grisebachstr. 8 D-3400 Göttingen Federal Republic of Germany Department of Biological Sciences University of Dundee DD1 4HN Dundee UK Abstract d -Ribulose 1,5-diphosphate carboxylase has been purified from autotrophically grown cells of the facultative chemolithotrophic hydrogen bacterium Alcaligenes eutrophus . The enzyme was homogeneous by the criteria of polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 505000 determined by gel filtration and sucrose density gradient centrifugation, and a sedimentation coefficient of 18.2 S was obtained. It was demonstrated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis that the enzyme consists of two types of subunits of molecular weight 52000 and 13000. Electron microscopy on the intact and the partially dissociated enzyme lead to the construction of a model for the quaternary structure of the enzyme which is composed of 8 large and 8 small subunits. The most probable symmetry of the enzyme molecule is 4:2:2. Michaelis constant ( K m ) values for ribulose 1,5-diphosphate, Mg 2- , and CO 2 were 0.59 mM, 0.33 mM, and 0.066 mM measured under air. Oxygen was a competitive inhibitor with respect to CO 2 suggesting that the enzyme also exhibits an oxygenase activity. The oxygenolytic cleavage of ribulose 1,5-diphosphate was shown and a 1:1 stoichiometry between oxygen consumption and 3-phosphoglycerate formation observed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

Purification, some properties and quaternary structure of the d -ribulose 1,5-diphosphate carboxylase of Alcaligenes eutrophus

Bowien, B.; Mayer, F.; Codd, G.; Schlegel, H.
Archives of Microbiology , Volume 110 (2) – Nov 1, 1976
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References (50)

Publisher
Springer Journals
Copyright
Copyright © 1976 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00690223
Publisher site
See Article on Publisher Site

Abstract

203 110 110 2 3 B. Bowien F. Mayer G. A. Codd H. G. Schlegel Institut für Mikrobiologie der Universität Grisebachstr. 8 D-3400 Göttingen Federal Republic of Germany der Gesellschaft für Strahlen-und Umweltforschung mbH Grisebachstr. 8 D-3400 Göttingen Federal Republic of Germany Department of Biological Sciences University of Dundee DD1 4HN Dundee UK Abstract d -Ribulose 1,5-diphosphate carboxylase has been purified from autotrophically grown cells of the facultative chemolithotrophic hydrogen bacterium Alcaligenes eutrophus . The enzyme was homogeneous by the criteria of polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 505000 determined by gel filtration and sucrose density gradient centrifugation, and a sedimentation coefficient of 18.2 S was obtained. It was demonstrated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis that the enzyme consists of two types of subunits of molecular weight 52000 and 13000. Electron microscopy on the intact and the partially dissociated enzyme lead to the construction of a model for the quaternary structure of the enzyme which is composed of 8 large and 8 small subunits. The most probable symmetry of the enzyme molecule is 4:2:2. Michaelis constant ( K m ) values for ribulose 1,5-diphosphate, Mg 2- , and CO 2 were 0.59 mM, 0.33 mM, and 0.066 mM measured under air. Oxygen was a competitive inhibitor with respect to CO 2 suggesting that the enzyme also exhibits an oxygenase activity. The oxygenolytic cleavage of ribulose 1,5-diphosphate was shown and a 1:1 stoichiometry between oxygen consumption and 3-phosphoglycerate formation observed.

Journal

Archives of Microbiology – Springer Journals

Published: Nov 1, 1976

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