Document Type

Article

Publication Date

4-18-2008

Department

Chemistry and Biochemistry

Abstract

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 fixation reaction confirmed the importance of a functional carboxysomal carbonic anhydrase for efficient catalysis by RubisCO. Furthermore, comparisons of the reaction in intact and broken microcompartments and by purified carboxysomal RubisCO implicated the protein shell of the microcompartment as impeding diffusion of CO2 into and out of the carboxysome interior.

Publication Title

Journal of Biological Chemistry

Volume

283

Issue

16

First Page

10377

Last Page

10384

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