Abstract

This dissertation examines the structure and function of photosynthetic proteins that contain c-type heme cofactors that function in the electron transport chains of anaerobic phototrophic bacteria. The diversity and range of these cytochromes proteins was explored. Then, individual proteins were studied in detail. The diheme cytochrome c from Heliobacteria modesticaldum was studied using hydrogen deuterium exchange mass spectrometry and homology modeling. A structural model of the protein and a mechanism for the cytochrome bc complex was proposed. Next, the monoheme cytochrome c subunit from the Alternative Complex III from the Filamentous Anoxygenic Phototrophs was studied using biochemistry and found to be a necessary subunit for enzyme activity. The structure of the Alternative Complex III was then studied with homology modeling and the interaction of the complex with its soluble electron acceptor auracyanin was studied. Next, the structure of the LHRC was studied using Electron Microscopy and the supramolecular organization of the complex was studied with Atomic Force Microscopy. The relationship between the Alternative Complex III and the LHRC was also explored. A model of the FAP photosynthetic membrane was proposed. Several individual cytochromes were analyzed to understand their structure, function and mechanisms.

Committee Chair

Robert E Blankenship

Committee Members

Dewey Holten, Liviu Mirica, Michael Gross, Robert Kranz,

Comments

Permanent URL: https://doi.org/10.7936/K71V5C5V

Degree

Doctor of Philosophy (PhD)

Author's Department

Chemistry

Author's School

Graduate School of Arts and Sciences

Document Type

Dissertation

Date of Award

Summer 8-15-2015

Language

English (en)

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