Abstract：
:Yeast enolase is stabilized by its natural cofactor Mg(2+). This stabilization is ascribed to the reduced subunit dissociation of the holoprotein. Nevertheless, how Mg(2+) alters the unfolding mechanism has yet to be fully characterized. Here, we investigate the role of Mg(2+) in the denaturation mechanism and unfolding kinetics of yeast enolase. Apo-enolase unfolds through a three-state process (N(2)↔2I→2D). The intermediate species is described as a monomeric molten globule-like conformation that becomes noticeable in the presence of phosphate and is able to recover its native secondary structure when cooled down. Kinetic studies confirmed the presence of the intermediate species, even though it was not noticeable in the thermal scans. The cofactor increases the cooperativity of the unfolding transitions, while the intermediate species becomes less noticeable or nonexistent. Thus, holo-enolase follows a simple two-state mechanism (N(2)→2D). Our results indicate smaller unfolding rate-constants in the presence of Mg(2+), thus favoring the native state. The temperature dependence of the unfolding rates allowed us to calculate the activation enthalpies of denaturation. Interestingly, despite the different unfolding mechanisms of the apo and holo forms of enolase, they both have similar activation barriers of denaturation (185-190 kJ mol(-1)).
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Moreno-Vargas LM,Carrillo-Ibarra N,Arzeta-Pino L,Benítez-Cardoza CGdoi
10.1016/j.ijbiomac.2011.07.021subject
Has Abstractpub_date
2011-12-01 00:00:00pages
871-8issue
5eissn
0141-8130issn
1879-0003pii
S0141-8130(11)00299-6journal_volume
49pub_type
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