Thermal properties and oxygenase activity of ribulose-1,5-bisphosphate carboxylase from the thermophilic purple bacterium, Chromatium tepidum |
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| Authors: | Ghanshyam D Heda Michael T Madigan |
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| Institution: | Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA;Department of Microbiology, Southern Illinois University, Carbondale, IL, U.S.A. |
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| Abstract: | Abstract Ribulose-1,5-biphosphate carboxylase (RuBPCase) partially purified from the thermophilic purple bacterium Chromatium tepidum displayed maximum carboxylase activity at 50°C, while enzyme from a related mesophilic species, Chromatium vinosum , was completely inactive at 50°C. RuBPCase from C. tepidum showed ribulose-1,5- bisphosphate-dependent oxygenase activity, and, in addition, O2 was found to partially destroy carboxylase activity. It is concluded that thermophilic purple bacteria produce heat-stable RuBPCase and that all RuBPCases, even those from an obligate anaerobe such as C. tepidum , have associated oxygenase activity. |
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| Keywords: | Purple bacterium Ribulose-1 5-bisphosphate carboxylase Thermophily |
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