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Mechanism of the Molecular Interaction between Cerium (III) and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco)
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Mechanism of the Molecular Interaction between Cerium (III) and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco)
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Journal Article
Mechanism of the Molecular Interaction between Cerium (III) and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco)
2011
Overview
The mechanism of the molecular interaction between Ce3+, a member of rare earth elements, and Rubisco in vitro is investigated. The carboxylase activity of Rubisco greatly increased under low concentrations of Ce3+ and decreased under high concentrations of Ce3+. The ultraviolet absorption spectra show that the various concentrations of Ce3+ treatment do not shift the characteristic peaks of Rubisco while the characteristic peak intensity of Rubisco increases with increasing Ce3+ concentration. The Rubisco–Ce3+ interactions also do not cause any noticeable change in the λmax of Rubisco fluorescence spectra. However, the fluorescence intensity of Rubisco is found quenched by the addition of Ce3+, which strongly suggests that Ce3+ could directly bind to the Rubisco protein. and the binding sites is estimated to 1.52 per protein. The binding between Ce3+ and Rubisco is also proved by extended X-ray absorption fine-structure essay; Ce3+ coordinated with eight oxygen atoms of Rubisco in first shells and six oxygen atoms in second shells. The results implied that Ce3+ might improve the microenvironment of Rubisco and, in turn, affected the carboxylase capacity of Rubisco greatly.
Publisher
Springer-Verlag,Humana Press Inc,Springer Nature B.V
