2026-09-21T08:06:54Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/84482 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

Lu, Yi Gengenbach, Alan James 2015-09-25T22:14:45Z 2015-09-25T22:14:45Z 10000-01-01 2000 2000 The active site tryptophans were removed from MnCcP in order to investigate the roles of Trp51 and Trp191 in MnP activity. These residues are phenyalanines in MnP. In CcP mutants without the Mn(II)-binding site, Trp191 and Trp51 greatly influence the lifetime of the porphyrin pi-cation radical. The W51F, W191F, and W51F/W191F double mutations were incorporated along with the binding-site mutations (G41E,V45E,H181D) to create MnCcP(W51F), MnCcP(W191F) and MnCcP(W51F, W191F). The MnP activity observed varied between mutants and increased activity was observed for MnCcP(W51F,W191F) and MnCcP(W51F). The trend in activity reflects the extent of compound II stabilization present for the various mutants. MnC cP(W51F,W191F) is the most active protein model of MnP constructed to date. Made available in DSpace on 2015-09-25T22:14:45Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9990003.pdf: 5897619 bytes, checksum: a22ee3786f07ab43564774c9d67a08b6 (MD5) Previous issue date: 2000 Embargo set by: Seth Robbins for item 85763 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 139 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000. http://hdl.handle.net/2142/84482 (MiAaPQ)AAI9990003 eng Chemistry, Biochemistry The Protein Redesign Approach to Modeling Manganese Peroxidase text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.