Biochemical Studies of the Sodium -Translocating NADH:ubiquinone Oxidoreductase

In the NqrF subunit, four conserved cysteines (C70, C76, C79 and C111) are predicted to ligate the 2Fe-2S center, and three conserved residues (R210, Y212, S245) are predicted to be essential to the binding of the FAD cofactor. By mutagenesis and spectroscopic characterization, the four conserved cysteines are confirmed to be the ligands for the 2Fe-2S center, and R210, Y212, S245 are confirmed to be important for the binding of the FAD cofactor in Na +-NQR. Functional studies on these mutants strongly support an electron transport pathway model in which the non-covalently bound FAD in the NqrF subunit is the first redox cofactor to take electrons from the substrate, NADH, and that the electrons then flow to the 2Fe-2S center.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Zhou, Weidong

Contributors dc:contributor

• Gennis, Robert B.

• Biophysics, General

Language dc:language

eng

Identifier

(MiAaPQ)AAI3044275

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84783