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Frauenfelder, Hans Good, David Eckert 2011-06-16T16:06:07Z 2011-06-16T16:06:07Z 10000-01-01 1981 Infrared spectra of carbon monoxide bound myoglobin reveal several lines due only to the carbon monoxide. Studies with isotopically enriched CO confirm the assignment of these lines. After photodissociation, the lines shift and change in extinction coefficient, giving an indication of the nature of the neighborhood of the photodissociated CO. At temperatures between 10K and lOOK three different CO environments are seen after photodissociation, with relative populations depending on temperature. Two forms are found to be weakly bound to the protein, but not at the iron center. The third form moves freely within a cavity formed by the protein structure. The binding entha1pies relative to the third form have been determined. Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-16T16:06:07Z No. of bitstreams: 1 1981_good.pdf: 1615959 bytes, checksum: d2c33f21f36013261b3289114d4f905c (MD5) Made available in DSpace on 2011-06-16T16:06:07Z (GMT). No. of bitstreams: 1 1981_good.pdf: 1615959 bytes, checksum: d2c33f21f36013261b3289114d4f905c (MD5) Previous issue date: 1981 Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-16T16:06:07Z Item is restricted indefinitely. Restriction data tranferred 2014-07-01T11:13:03-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis Thesis U of I Only 487673 http://hdl.handle.net/2142/25428 en 1981 David Eckert Good infrared spectroscopy photodissociated carboxymyoglobin myoglobin Infrared spectroscopy of photodissociated carboxymyoglobin Dissertation / Thesis text Physics Physics University of Illinois at Urbana-Champaign Dissertation Ph.D.