NDLI: Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix

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Extremophiles : Volume 14, Issue 1, January 2010

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Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix

Content Provider	Springer Nature Link
Author	Karlström, Mikael Chiaraluce, Roberta Giangiacomo, Laura Steen, Ida Helene Birkeland, Nils Kåre Ladenstein, Rudolf Consalvi, Valerio
Copyright Year	2010
Abstract	The multi-domain enzyme isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix was studied by denaturant-induced unfolding. At pH 7.5, changes in circular dichroism ellipticity and intrinsic fluorescence showed a complex unfolding transition, whereas at pH 3.0, an apparently two-state and highly reversible unfolding occurred. Analytical ultracentrifugation revealed the dissociation from dimer to monomer at pH 3.0. The thermodynamic and kinetic stability were studied at pH 3.0 to explore the role of inter-domain interactions independently of inter-subunit interplay on the wild type and R211M, a mutant where a seven-membered inter-domain ionic network has been disrupted. The unfolding and folding transitions occurred at slightly different denaturant concentrations even after prolonged equilibration time. The difference between the folding and the unfolding profiles was decreased in the mutant R211M. The apparent Gibbs free energy decreased approximately 2 kcal/mol and the unfolding rate increased 4.3-fold in the mutant protein, corresponding to a decrease in activation free energy of unfolding of 0.86 kcal/mol. These results suggest that the inter-domain ionic network might be responsible for additional stabilization through a significant kinetic barrier in the unfolding pathway that could also explain the larger difference observed between the folding and unfolding transitions of the wild type.
Starting Page	213
Ending Page	223
Page Count	11
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	14
Issue Number	2
e-ISSN	14334909
Language	English
Publisher	Springer Japan
Publisher Date	2010-01-08
Publisher Place	Japan
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Hyperthermophiles Protein stability Thermodynamic stability Kinetic stability Ionic networks Multi-domain protein Isocitrate dehydrogenase Ecology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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