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- Title
Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase
- Authors
Ordu, Emel B.; Cameron, Gus; Clarke, Anthony R.; Karagüler, Nevin Gül
- Abstract
Abstract: The folding mechanism and stability of dimeric formate dehydrogenase from Candida methylica was analysed by exposure to denaturing agents and to heat. Equilibrium denaturation data yielded a dissociation constant of about 10−13 M for assembly of the protein from unfolded chains and the kinetics of refolding and unfolding revealed that the overall process comprises two steps. In the first step a marginally stable folded monomeric state is formed at a rate (k 1) of about 2×10−3 s−1 (by deduction k −1 is about10−4 s−1) and assembles into the active dimeric state with a bimolecular rate constant (k 2) of about 2×104 M−1 s−1. The rate of dissociation of the dimeric state in physiological conditions is extremely slow (k −2 ∼3×10−7 s−1).
- Subjects
THERMODYNAMICS; PROTEIN folding; DEHYDROGENASES; DIMERS; CANDIDA; DENATURATION of proteins; DATA analysis; HEAT
- Publication
FEBS Letters, 2009, Vol 583, Issue 17, p2887
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.07.048