A stochastic attractor participates in chymotrypsin catalysis. A new facet of enzyme catalysis

✍ Scribed by Bent H. Havsteen

• Publisher: Elsevier Science
• Year: 1991
• Tongue: English
• Weight: 816 KB
• Volume: 151
• Category: Article
• ISSN: 0022-5193
• DOI: 10.1016/s0022-5193(05)80370-4

✦ Synopsis

The previously observed discrete levels of vibrational parameters of chymotrypsin and tosyl-chymotrypsin were analyzed by the methods of non-linear dynamics in order to investigate their origin. The fractal dimensionality of the step sequence was determined using the correlation function and the Farey-tree method. These methods yielded the same value and indicated the presence of a "Devil's Staircase", i.e. the existence of a stochastic attractor. The latter was assigned to the substrate-mobilizable conformation. The attractor dimension of the catalytic site in the acylated state was found to be indistinguishable from that of the substrate mobilizable conformation. A "Devil's Staircase" signals the transition from the regular to the stochastic regime. This transition is shared by critical phenomena and may be a prerequisite for catalysis.