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The Influence of Pressure on The Low-Temperature Kinetics of Myoglobin text Sorensen, Larry Brice 2015-05-13T15:22:21Z 2015-05-13T15:22:21Z 10000-01-01 1980 1980 The recombination of carbon monoxide and dioxygen to horse and sperm whale myoglobin at low temperatures (60 - 160K) was studied using high pressure flash photolysis techniques. By comparing the pressure dependence when the system is first frozen and then pressurized with the pressure dependence when the system is first pressurized and then frozen, the total volume change for the reaction can be resolved into an activation volume component and a conformational volume component. Strong evidence requiring both conformational volume and activation volume components was found. Over the pressure range studied (0.1 - 200 MPa) the observed volume changes were independent of the applied pressure. At low temperatures, the recombination reaction must be described by a distribution of activation enthalpies. A simple configuration coordinate model was developed which predicts distributions in excellent agreement with the observed distributions. Made available in DSpace on 2015-05-13T15:22:21Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 8026599.PDF: 2994195 bytes, checksum: c9dcade42a6e13c6987b2584e08581b1 (MD5) Previous issue date: 1980 Embargo set by: Seth Robbins for item 78399 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 155 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1980. http://hdl.handle.net/2142/77188 (UMI)AAI8026599 eng Physics, Molecular Physics Physics University of Illinois at Urbana-Champaign Dissertation Ph.D.