title: Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase.
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 2x10(-3)s(-1) (by deduction k(-1) is about 10(-4)s(-1)) and assembles into the active dimeric state with a bimolecular rate constant (k(2)) of about 2x10(4)M(-1)s(-1). The rate of dissociation of the dimeric state in physiological conditions is extremely slow (k(-2) approximately 3x10(-7)s(-1)).
authors: Istanbul Technical University, Faculty of Science and Letters, Department of Molecular Biology and Genetics, Istanbul, Turkey.
authors: Emel B
authors: EB
authors: Ordu
authors: Gus
authors: G
authors: Cameron
authors: Anthony R
authors: AR
authors: Clarke
authors: Nevin Gül
authors: NG
authors: Karagüler
mesh_terms: D002175:Candida / Q000201:enzymology; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D007700:Kinetics; D011489:Protein Denaturation; D017510:Protein Folding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D013816:Thermodynamics
chemical_list: D005656:Fungal Proteins; D005560:Formate Dehydrogenases