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Entropic Contributions to Rate Accelerations in Enzymic and Intramolecular Reactions and the Chelate Effect
Open accessAbstract
It is pointed out that translational and (overall) rotational motions provide the important entropic driving force for enzymic and intramolecular rate accelerations and the chelate effect; internal rotations and unusually severe orientational requirements are generally of secondary importance. The loss of translational and (overall) rotational entropy for 2 → 1 reactions in solution is ordinarily on the order of 45 entropy units (e.u.) (standard state 1 M, 25°C); the translational entropy is much larger than 8 e.u. (corresponding to 55 M). Low-frequency motions in products and transition states, about 17 e.u. for cyclopentadiene dimerization, partially compensate for this loss, but “effective concentrations” on the order of 10 8 M may be accounted for without the introduction of new chemical concepts or terms.
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“Mielke and coworkers (2011) argued that these micro- and nanocompartments would restrict diffusion of hydrothermal fluids and thereby focus reactions with the invasive carbonic ocean at, or within, their boundaries ‘‘and act as ‘low-entropy’ traps whereby compatible products would be forced to interact through their p…”
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Metadata
- Authors
- Page, M. I., & Jencks, W. P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1971-08
- Volume
- 68
- Issue
- 8
- Pages
- 1678-1683
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2072660673
- Cited by
- 1,014
- References
- 0
- FWCI
- 16.82
- Type
- journal article
- Language
- en
- Open access
- green
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