Unstable electron pairing and the energy loan model of enzyme catalysis
dc.contributor.author | Conrad, Michael | en_US |
dc.date.accessioned | 2006-04-07T17:33:38Z | |
dc.date.available | 2006-04-07T17:33:38Z | |
dc.date.issued | 1979-07-21 | en_US |
dc.identifier.citation | Conrad, M. (1979/07/21)."Unstable electron pairing and the energy loan model of enzyme catalysis." Journal of Theoretical Biology 79(2): 137-156. <http://hdl.handle.net/2027.42/23526> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WMD-4F1J831-60/2/9e828272690fd8edaf24e4bbc5925e45 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23526 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=513805&dopt=citation | en_US |
dc.description.abstract | A theory of enzyme catalysis is described which utilizes a thermodynamically consistent construction of a free energy diagram with different pathways for complex formation and decomposition. The switch to the decomposition pathway occurs when downward uncertainty and thermal fluctuations make possible a short-lived potential energy dominance in which parallel spin electrons are paired and thus free to drop below the energy floor normally maintained by the Pauli exclusion principle. Such pairing is possible if van der Waal's and other weak interactions holding the complex together impose confinement constraints on parallel spin electrons, thereby both increasing uncertainty fluctuations in their kinetic energy and weakly favoring a phase correlation in their motion (which can be interpreted in terms of an exchange of virtual particles). The paired configuration is highly unstable and thus energy released by pair falling is either immediately recaptured to re-establish a normal orbital structure or, if the pair persists long enough to produce a nuclear motion, recaptured at the end of this motion. In the latter case the release of energy can be thought of as an energy loan which finances the switch to the lower activation energy pathway without compromising an energy-balanced regeneration of the enzyme. The advantage is that the complex (because of its instability) has a real free energy which is lower than the free energy which would be assigned to it on the basis of its equilibrium concentration. This increases the specificity and speed of complex formation without decreasing the speed of decomposition. The theory predicts that the magnetic moment which marks the pair should accompany the nuclear (e.g. allosteric) motion and that the pair formation stage of the enzymatic process should have an anomalous temperature dependence. Variations of the model may be constructed to deal with a number of processes involving macromolecular motions, including sequential processes in catalysis, allosteric control, persistent molecular motions, self-assembly, energy transfer, channeled transport, and protection against inhibitors. | en_US |
dc.format.extent | 1215496 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Unstable electron pairing and the energy loan model of enzyme catalysis | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Computer and Communication Sciences, University of Michigan, Ann Arbor, Michigan 48104, U.S.A. | en_US |
dc.identifier.pmid | 513805 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23526/1/0000481.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0022-5193(79)90243-1 | en_US |
dc.identifier.source | Journal of Theoretical Biology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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