d-Ribulose 1,5-bisphosphate carboxylase of the nitrifying bacterium,<i>Nitrobacter agilis</i>

Harrison, D.; Rogers, Lyndon J.; Smith, A. J.

doi:10.1111/j.1574-6968.1979.tb04275.x

Cited by 4 publications

(1 citation statement)

References 23 publications

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“…However, heterogeneity of large subunits of C. tepidum RuBisCO, as evidenced by a shoulder on the single peak obtained in densitometric scans of purified enzyme on SDS/ PAGE gels (Fig.ZB), cannot be ruled out. Large-subunit heterogeneity in RuBisCO from several sources, including phototrophic purple bacteria [25], is not uncommon, and may be due to in vitro proteolytic cleavage [26,271. Torres-Ruiz and McFadden [3] observed similar heterogeneity, but with the small subunits of C. vinosum RuBisCO.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of the thermostable ribulose‐1,5‐bisphosphate carboxylase/oxygenase from the thermophilic purple bacterium Chromatium tepidum

Heda

Madigan

1989

European Journal of Biochemistry

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The Calvin cycle enzyme ribulose-bisphosphate carboxylase/oxygenase has been purified and characterized from the thermophilic and obligately anaerobic purple sulfur bacterium, Chromatium tepidum. The enzyme is an L8S8 carboxylase with a molecular mass near 550 kDa. N o evidence for a second form of the enzyme lacking small subunits was obtained. C. tepidum ribulose-bisphosphate carboxylase/oxygenase was stable to heating to temperatures of 60°C and could be readily purified in an active form at room temperature. Both carboxylase and oxygenase activities of this enzyme were Mg2 +-dependent and carboxylase activity was sensitive to the effector 6-phosphogluconic acid. The K , for ribulose bisphosphate for the carboxylase activity of the C. tepidurn enzyme was substantially higher than that observed in mesophilic Calvin cycle autotrophs. Amino acid composition and immunological analyses of C. tepidum and Chromatium vinosum ribulose-bisphosphate carboxylases showed the enzymes to be highly related despite significant differences in heat stability. It is hypothesized that thermal stability of C. tepidum ribulose-bisphosphate carboxylase/oxygenase is due to differences in primary structure affecting folding patterns in both the large and small subunits and is clearly not the result of any unique quaternary structure of the thermostable enzyme.Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) catalyzes the first step of C 0 2 fixation in organisms that employ the reductive pentose phosphate (Calvin) cycle in autotrophic metabolism [l]. Among phototrophic purple bacteria the Calvin cycle is universally distributed [l, 21. However, different molecular forms of RuBisCO varying in quaternary structure from the L& green-plant enzyme have been observed in certain species of purple bacteria [l, 21. Among purple sulfur bacteria, RuBisCO from Chromatium vinosum has been particularly well studied, as the native enzyme is an form and can be easily purified and obtained in large amounts [3]. Recent studies of C. vinosum RuBisCO have shown that a catalytically active L8 form of the enzyme can be generated from the native L8S8 form [4]. The ease of obtaining pure preparations of both forms of the enzyme from C. vinosum has focused efforts towards defining the role of small subunits in the overall reaction sequence. Thus far, it appears clear that RuBisCO small subunits have no catalytic functions but may play a regulatory role in promoting activation of the intact enzyme [5, 61. Recently, a thermophilic species of Chromatium, Chromatium tepidurn, was isolated by our laboratory [7,8] and shown to fix CO, via the Calvin cycle [9]. Reflecting its hot-spring origin, C. tepidum was shown to produce a thermally active RuBisCO with a temperature optimum of 50°C [9]. In order to relate these thermal properties to other physical properties Correspondence to M . T. Madigan, Department of Microbiology, Ahhreviations. Ribulose-P,, ribulose-l,5-bisphosphate; RuBisCO, Enzyme. Ribulose-I ,5-bisphosphate carboxylase/oxygenase (EC

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of the thermostable ribulose‐1,5‐bisphosphate carboxylase/oxygenase from the thermophilic purple bacterium Chromatium tepidum

Heda

Madigan

1989

European Journal of Biochemistry

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Ribulose-1,5-bisphosphate carboxylase/oxygenase from a nitrite-oxidizing chemoautotroph, Nitrobacter agilis ATCC 14123: Purification and properties

Masuko

Takahashi

Fujioka

et al. 1996

Journal of Fermentation and Bioengineering

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The Carboxysomes (Polyhedral Bodies) of Autotrophic Prokarygtes

Codd¹,

Marsden²

1984

Biological Reviews

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Summary 1. Polyhedral bodies are present in several groups of autotrophic bacteria that assimilate inorganic carbon via the Calvin cycle, including members of the colourless sulphur‐ oxidizing bacteria, ammonia‐ and nitrite‐oxidizing bacteria and all cyanobacteria (blue‐green algae) examined. Other groups of Calvin‐cycle bacteria lack the inclusions, which have not been found in the purple photosynthetic bacteria, or in the hydrogen bacteria, with one exception in each case. Polyhedral bodies also occur in the chlorophyll b‐containing photosynthetic symbiotic prokaryote, Prochloron, and in several cyanelles. The inclusion bodies have not been found in prokaryotes that cannot fix carbon dioxide via the Calvin cycle, or in eukaryotes. 2. Polyhedral bodies have been isolated from a colourless sulphur bacterium (Thiobacillus neapolitanus), two nitrifying bacteria (Nitrobacter agilis and Nitrosomonas sp.) and two cyanobacteria (Anabaena cylindrica and Chlorogloeopsis fritschii). Ribulose 1,5‐bisphosphate carboxylase/oxygenase (RuBisCO), the carbon dioxide‐fixing enzyme of the Calvin cycle, has been found in the polyhedral bodies in each case, confirming that these inclusions in autotrophic bacteria be re‐termed carboxysomes. 3. Knowledge of carboxysome composition has been constrained by difficulties in carboxysome isolation, although effective methods, including cell disruption in low‐ionic‐strength buffers followed by density‐gradient centrifugation through silicon polymers, or sucrose, followed be preparative agarose electrophoresis, are now available. 4. Analysis of isolated T. neapolitanus, N. agilis and C. fritschii carboxysomes by dissociating sodium dodecyl sulphate‐polyacrylamide gel electrophoresis has revealed the presence of 7–15 polypeptides, the most abundant being the large and small subunits of RuBisCO. Two polypeptides of the T. neapolitanus carboxysomes have been ascribed to the carboxysome membrane (shell), although the identity of other polypeptides is unknown. 5. DNA of unknown function has been reported in carboxysomes isolated from two Nitrobacter species and may be present in the organelles from T. neapolitanus. 6. RuBisCO occurs in both the carboxysomes and in soluble form in the cytoplasm of carboxysome‐containing bacteria. Structural, kinetic, regulatory and immunological comparisons have demonstrated full or near identity between the cytoplasmic and carboxysomal forms of the enzyme. As with RuBisCO from chloroplasts and from almost all non‐carboxysome‐containing bacteria, the cytoplasmic and carboxysomal RuBisCOs each consist of eight large plus eight small subunits. All RuBisCOs are bifunctional enzymes, oxygen acting as a competitive inhibitor of carboxylation, and carbon dioxide acting competitively to inhibit the apparently wasteful oxygenase reaction. Carbon dioxide and oxygen fixation occur at the same site on the large subunit. Despite extensive study, the function of the small subunits is unknown. All RuBisCOs can exist in an inactive and active form, activation proceeding by an ord...

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d-Ribulose 1,5-bisphosphate carboxylase of the nitrifying bacterium,Nitrobacter agilis

Cited by 4 publications

References 23 publications

Purification and characterization of the thermostable ribulose‐1,5‐bisphosphate carboxylase/oxygenase from the thermophilic purple bacterium Chromatium tepidum

Purification and characterization of the thermostable ribulose‐1,5‐bisphosphate carboxylase/oxygenase from the thermophilic purple bacterium Chromatium tepidum

Ribulose-1,5-bisphosphate carboxylase/oxygenase from a nitrite-oxidizing chemoautotroph, Nitrobacter agilis ATCC 14123: Purification and properties

The Carboxysomes (Polyhedral Bodies) of Autotrophic Prokarygtes

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