Ligand Binding and Structural Dynamics in C-Type Cytochromes

The first molecular dynamic simulations of the interaction of cyt c and yeast bc1 complex are described. Contrary to results from crystallographic studies, the simulations reveal multiple dynamic hydrogen bonds and salt bridges in the cyt c-c 1 interface. A novel structural change in cyt c is also reported, involving residues 25--30, which may be responsible for cyt c destabilization. An interaction between cyt c1 monomers is proposed to be responsible for limiting the binding of cyt c to only one molecule per bc 1 dimer by altering the affinity of the cytochrome c binding site on the second cyt c1 monomer. A mechanism is also proposed explaining changes in cyt c binding affinity related to the position of the headgroup of the iron-sulfur protein.

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

• Kokhan, Oleksandr

Contributors dc:contributor

• Wraight, Colin A.

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI3392097

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/85477