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oai:www.ideals.illinois.edu:2142/84846 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Lu, Yi Wang, Ningyan 2015-09-25T22:28:10Z 2015-09-25T22:28:10Z 10000-01-01 2007 2007 Novel oxygen reactivity is observed in our model protein (CuBMb) which reproduces the most essential components of HCO active site. In order to improve this artificial model to inhibit its side reaction with oxygen and channel it toward oxidase reactivity, more features were introduced into the CuBMb model in this study: (1) synthetic heme cofactors are used to replace the natural one of the protein, resulting in ∼20 fold inhibition of the side reaction; (2) a novel semi-synthetic system (Expressed Protein Ligation) is also established that may introduce new features such as the Tyr-His cross-linking structure in HCO to the model by direct incorporation of unnatural amino acid(s) into the protein sequence. These strategies demonstrate the power of combining the strength of biological, chemical and modern analytical techniques to create accurate biosynthesis models of protein active sites which can provide insight not easily achievable through other studies, thereby complementing the knowledge gained from both native protein and synthetic model studies. Made available in DSpace on 2015-09-25T22:28:10Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3290422.pdf: 2849859 bytes, checksum: b79a50a17a945c65419792ab15f926a2 (MD5) Previous issue date: 2007 Embargo set by: Seth Robbins for item 86127 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 129 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007. http://hdl.handle.net/2142/84846 (MiAaPQ)AAI3290422 eng Chemistry, Biochemistry Exploring the Roles of Heme Type and Histidine -Tyrosine Cross -Link in Heme-Copper Oxidases Using a Myoglobin Model text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.