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oai:www.ideals.illinois.edu:2142/84091 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

van der Donk, Wilfred A. Vrtis, Jennifer Marie 2015-09-25T22:12:50Z 2015-09-25T22:12:50Z 10000-01-01 2002 2002 Cytochrome c oxidase, an enzyme that catalyzes the reduction of oxygen to water, has a binuclear center as well as a unique post-translational modification in the active site. Specifically, there is a crosslink between the nitrogen (Nepsilon2) of His240 and the carbon (Cepsilon 2) of Tyr244 (numbers correspond to CcO from bovine heart). The significance of the linkage was investigated by comparing the physicochemical properties of a model compound, 2-(imidazolyl-1-yl-4-methylphenol) to p-cresol. Made available in DSpace on 2015-09-25T22:12:50Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3070466.pdf: 5856660 bytes, checksum: 706fcadf61a6c5f83ce91bbcc342a817 (MD5) Previous issue date: 2002 Embargo set by: Seth Robbins for item 85372 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 134 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2002. http://hdl.handle.net/2142/84091 (MiAaPQ)AAI3070466 eng Chemistry, Organic Mechanistic Studies and Synthetic Applications of Phosphite Dehydrogenase text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.