Molecular genetic manipulation and characterization of the high-potential chain of cyclic electron transport in Rhodobacter sphaeroides

The Rieske iron-sulfur subunit of the cytochrome bc$\sb{1}$ complex of Rhodobacter sphaeroides assembles in the E. coli and R. sphaerodies membranes with its iron-sulfur cluster intact, in the absence of the cytochrome subunits. This assembly, in light of predicted structural features of the hydrophobic amino-terminus and proteolytic release of a soluble domain, suggests the subunit may be anchored to the membrane by a single amino-terminal, transmembrane helix. Sequence homology with dioxygenase subunits binding a spectrally similar 2FE-2S cluster, suggests the fully conserved residues of the cytochrome bc$\sb{1}$ and b$\sb{6}$f sequences ligating the iron-sulfur cluster may be the first and third cysteines and both histidines. When Gly133, neighboring the ligands of the cluster, is replaced by aspartate, quinol oxidation is specifically impaired at the Q$\sb{\rm o}$ site.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biophysics

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Van Doren, Steven R.

Contributors dc:contributor

• Crofts, Antony R.

• Chemistry, Biochemistry
• Biophysics, General

Statement dc:rights

• Copyright 1991 Van Doren, Steven R.

Language dc:language

eng

Identifier

AAI9211020
(UMI)AAI9211020

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/21248