Exploring the Quinol Oxidation Mechanism at the Qo-Site of Bc1 Complex Through Site-Directed Mutagenesis

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biophysics and Computational Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Lhee, Sangmoon

Contributors dc:contributor

• Crofts, Antony R.

• Biology, Microbiology

Language dc:language

eng

Identifier

(MiAaPQ)AAI3301179

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/85465