2026-09-22T01:12:46Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/85465 2023-07-11 col_2142_5131 col_2142_14828 com_2142_5130 com_2142_14827 com_2142_14793 com_2142_8903

Crofts, Antony R. Lhee, Sangmoon 2015-09-25T22:46:11Z 2015-09-25T22:46:11Z 10000-01-01 2007 2007 The backbone amide groups of FL132 and FC134 give additional electron withdrawing force to the Rieske-type [2Fe-2S] cluster and the residues in the 132-134 positions play roles in anchoring the ISP to the surface of the Qo-pocket. FG133 has unique ϕ/psi angles that restrict the positions of two adjacent residues, FL132 and FC134, determining the favorable hydrogen bonds to the S2 of the cluster. A preliminary X-ray crystallographic study of FG133S showed the alterations in the hydrogen bond pattern surrounding the cluster and the flexible disulfide bridge between FC134 and FC151 by changing the ϕ/psi angles of FG133. Several mutant ISP's at FG133 and FL132 were prepared for investigating the flexibility in the backbone structure and the modifications in electrochemical parameters. Made available in DSpace on 2015-09-25T22:46:11Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3301179.pdf: 4659053 bytes, checksum: 7696771785cedd7d6b20f90ad984c630 (MD5) Previous issue date: 2007 Embargo set by: Seth Robbins for item 86746 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/2142/85465 (MiAaPQ)AAI3301179 eng Biology, Microbiology Exploring the Quinol Oxidation Mechanism at the Qo-Site of Bc1 Complex Through Site-Directed Mutagenesis text Biophysics and Computational Biology Biophysics and Computational Biology University of Illinois at Urbana-Champaign Dissertation Ph.D.