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Frauenfelder, Hans Johnson, Jeffrey Bruce 2011-05-12T16:41:55Z 2011-05-12T16:41:55Z 10000-01-01 1991 "When the structure of myoglobin was first revealed by x-ray crystallography, it was discovered that there was no clear evidence of a pathway for ligands to enter the protein to bind at the heme iron. Motions within the protein are necessary for the protein to function. Pressure release and flash photolysis experiments help characterize some of these protein motions. Sperm whale carbonmonoxymyoglobin exhibits three spectroscopically distinguishable carbon monoxide stretch bands between 1910 cm-1 and 1990 cm-1 labeled A0 , Ah and A3 . Pressure release measurements reveal three relaxations in the protein which are measured by: (1) the shifting in frequency of Ao, and the exchanges (2) A1 --+ A3, and (3) Ao --+ A1 + A3. Each relaxation is non-Arrhenius and solvent viscosity dependent. The rebinding of the A substates was observed after flash photolysis by monitoring the Soret band and the A substates. The low-temperature rebinding (20K-160K) exhibit increasing rebinding rates with increasing temperature. The three A substates show different rebinding rates. From ""' 170K to ""' 220K, the rebinding rate decreases with increasing temperature in each A substate. Between 220K and ""' 300K, the absorbance change of Ao is non-monotonic in time due to an interconversion between Ao and A1 + A3 during rebinding. This interconversion rate matches well with the extrapolated interconversion rate deduced from pressure release measurements. Since the three A substates have different rebinding rates, it is possible that the binding process is controlled in part by the interconversion between A substates. The maximum entropy method applied to the rebinding data reveals five peaks in the distribution of rebinding rates, labeled (from fast to slow) 1,2,3,E, and S. Peak 1 is due to geminate rebinding. Peaks 2 and 3 are well characterized, but not well understood. Peak 2 is present in all the A substates (except possibly A3 ) with the same rate as peak 2 monitored in the Soret. Peak 3 is the same in the Soret, A1 and likely A3 , however, it is absent in Ao. Peak 3 matches closely with the extrapolated interconversion between A1 and A3 and the shifting of peak frequency of Ao measured in pressure release experiments. PeakE is due to the interconversion Ao --+ A 1 + A3 and peak S arises from the rebinding of CO from the solvent." Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-05-12T16:41:55Z No. of bitstreams: 1 1991_Johnson.pdf: 1978604 bytes, checksum: 6e01611952b261bc4f99c5602bd5f2d4 (MD5) Made available in DSpace on 2011-05-12T16:41:55Z (GMT). No. of bitstreams: 1 1991_Johnson.pdf: 1978604 bytes, checksum: 6e01611952b261bc4f99c5602bd5f2d4 (MD5) Previous issue date: 1991 Restriction data tranferred 2014-07-01T11:13:57-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-05-12T16:41:55Z Item is restricted indefinitely. Thesis U of I Only 3480197 http://hdl.handle.net/2142/23877 en 1991 Jeffrey Bruce Johnson myoglobin protein motions ligand binding pressure release flash photolysis Motions in myoglobin Dissertation / Thesis text Physics Physics University of Illinois at Urbana-Champaign Dissertation Ph.D.