Exploring the Quinol Oxidation Mechanism at the Qo-Site of Bc1 Complex Through Site-Directed Mutagenesis
Lhee, Sangmoon
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https://hdl.handle.net/2142/85465
Description
Title
Exploring the Quinol Oxidation Mechanism at the Qo-Site of Bc1 Complex Through Site-Directed Mutagenesis
Author(s)
Lhee, Sangmoon
Issue Date
2007
Doctoral Committee Chair(s)
Crofts, Antony R.
Department of Study
Biophysics and Computational Biology
Discipline
Biophysics and Computational Biology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Microbiology
Language
eng
Abstract
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.
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