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Full-Text Articles in Physical Sciences and Mathematics
Halothiobacillus Neapolitanus Carboxysomes Sequester Heterologous And Chimeric Rubisco Species, Balaraj B. Menon, Zhicheng Dou, Sabine Heinhorst, Jessup M. Shively, Gordon C. Cannon
Halothiobacillus Neapolitanus Carboxysomes Sequester Heterologous And Chimeric Rubisco Species, Balaraj B. Menon, Zhicheng Dou, Sabine Heinhorst, Jessup M. Shively, Gordon C. Cannon
Faculty Publications
Background: The carboxysome is a bacterial microcompartment that consists of a polyhedral protein shell filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO), the enzyme that catalyzes the first step of CO(2) fixation via the Calvin-Benson-Bassham cycle. Methodology/Principal Findings: To analyze the role of RubisCO in carboxysome biogenesis in vivo we have created a series of Halothiobacillus neapolitanus RubisCO mutants. We identified the large subunit of the enzyme as an important determinant for its sequestration into alpha-carboxysomes and found that the carboxysomes of H. neapolitanus readily incorporate chimeric and heterologous RubisCO species. Intriguingly, a mutant lacking carboxysomal RubisCO assembles empty carboxysome shells of …
Co2 Fixation Kinetics Of Halothiobacillus Neapolitanus Mutant Carboxysomes Lacking Carbonic Anhydrase Suggest The Shell Acts As A Diffusional Barrier For Co2, Zhicheng Dou, Sabine Heinhorst, Eric B. Williams, C. Daniel Murin, Jessup M. Shively, Gordon C. Cannon
Co2 Fixation Kinetics Of Halothiobacillus Neapolitanus Mutant Carboxysomes Lacking Carbonic Anhydrase Suggest The Shell Acts As A Diffusional Barrier For Co2, Zhicheng Dou, Sabine Heinhorst, Eric B. Williams, C. Daniel Murin, Jessup M. Shively, Gordon C. Cannon
Faculty Publications
The widely accepted models for the role of carboxysomes in the carbon-concentrating mechanism of autotrophic bacteria predict the carboxysomal carbonic anhydrase to be a crucial component. The enzyme is thought to dehydrate abundant cytosolic bicarbonate and provide ribulose 1.5-bisphosphate carboxylase/oxygenase (RubisCO) sequestered within the carboxysome with sufficiently high concentrations of its substrate, CO2, to permit its efficient fixation onto ribulose 1,5-bisphosphate. In this study, structure and function of carboxysomes purified from wild type Halothiobacillus neapolitanus and from a high CO2-requiring mutant that is devoid of carboxysomal carbonic anhydrase were compared. The kinetic constants for the carbon …
Tetra-μ-Aqua-Octaaquabis(μ-4-Chloropyridine-2,6-Dicarboxylato(Bis(4-Chloro-Pyridine-2,6-Dicarboxylato)Tricobalt(Ii)-Disodium(I) Bis[Triaquabis(4-Chloro-Pyridine-2,6-Dicarboxylato)Cobalt(Ii)] Hexahydrate, Lamaryet Moody, Shawna Balof, Shanika Smith, Varma H. Rambaran, Don Vanderveer, Alvin A. Holder
Tetra-μ-Aqua-Octaaquabis(μ-4-Chloropyridine-2,6-Dicarboxylato(Bis(4-Chloro-Pyridine-2,6-Dicarboxylato)Tricobalt(Ii)-Disodium(I) Bis[Triaquabis(4-Chloro-Pyridine-2,6-Dicarboxylato)Cobalt(Ii)] Hexahydrate, Lamaryet Moody, Shawna Balof, Shanika Smith, Varma H. Rambaran, Don Vanderveer, Alvin A. Holder
Faculty Publications
The title compound, [Co3Na2(C72ClNO4)4(H2O)12][Co(C7H2ClNO4(H2O)3]2·6H2O, consists of a centrosymmetric dimer of [CoII(dipicCl)2]2- complex dianions [dipicCl is 4-chloropyridine-2,6-dicarboxylate] bridged by an [Na2CoII(H2O)12]4+ tetracationic cluster, two independent [Co(dipicCl)(H2O)3] complexes, and six water molecules of crystallization. The metals are all six-coordinate with distorted octahedral geometries. The [CoII(dipicCl)(H2O)3] complexes are neutral, with …