Interdisciplinary Plant Group

Photosynthesis is a dynamic process as plants must adapt from having too little to having too much light in relatively short time frames. Thus, these organisms must regulate solar capture from increasing efficiency to make a living to throttling back when excessive light may be harmful. While many of these modifications are understood at the molecular and systems biological levels, very little is understood at the biophysical level (i.e. what forces actually do the work). For instance, it is easy to say a membrane protein is phosphorylated or glycosylated and then moves in a membrane or is repaired, but how does the protein move? How does it get “repaired”? What the driving forces involved? These are very basic questions that can be asked of any cellular membrane, but whose answers have implications to virtually all photosynthetic and medically relevant processes.

My laboratory is interested in understanding what role the forces associated with protein-lipid interactions help to enact the myriad of functions that proteins play in and around a lipid bilayer (a.k.a. membrane). The questions we ask are often ones of import to how phototrophs harvest light, such as what makes a membrane protein stable and how does it decide where in a membrane system it should be located. We then try to apply the fundamental principles we and others are elucidating to specific questions of how do proteins get to their final destination in a membrane, how do they move in response to cellular stimuli, how are they repaired or replaced, and how do the membrane properties influence a proteins function. We carry out these studies in the hopes of understanding how we may be able to improve photosynthetic efficiency in various photosynthetic species or even in helping us to envision creating artificial bio-hybrid system for solar capture.

Currently, there are three main areas of research in the laboratory relating to plants:

1. What properties of a membrane, the physiochemical makeup of a membrane (a.k.a. its charge, thickness and fluidity), influence the stability or locale of a photosynthetic membrane protein in the thylakoid membrane.
2. What role does structural dynamics or structural stability play in the bioenergetic processes of photosynthetic and respiratory membrane proteins?
3. How do nascent proteins get folded and inserted into membranes during photosynthetic membrane biogenesis and repair.

• 2012 - Editorial Board, ISRN Structural Biology
• 2011 - Review Advisory Board, Frontiers in Microbial Physiology
• 2011 - Local Organizing Committee Member, International Congress on Photosynthesis Research, Summer 2013, St. Louis, MO
• 2009 Conference Organizer, 36th Midwest/Southeast Regional Photosynthesis Meeting, Turkey Run, IN
• 2008 Chair, University of Missouri local section of the American Chemical Society
• 2006 American Heart Association, Outstanding Research Recognition, top 5% of all scored proposals
• 2005-2006 American Heart Association Individual Postdoctoral Award, Mid-Atlantic Division
• 2003 NIH/NIGMS New Investigator Award, Gordon Research Conferences (Photosynthesis)
• 2002-2004 Ruth L. Kirschstein National Research Service Award
• 1999 NSF/DOE Award to Attend Microbial Physiology Workshop, Ohio State University
• 1996-2001 NSF Graduate Research Training Awardee: Early Events in Photosynthesis

C. M. Halsey, D. A. Benham, R. D. JiJi and J. W. Cooley (2012) "Influence of the lipid environment on valinomycin structure and cation complex formation" Spectrochimica Acta A Biomolecular Spectroscopy 96C:200-206

C. M. Halsey, O. Oshokoya, O. Johnson, S. Shinde, J. T. Beatty, G. Ghirlanda, R. D. JiJi, and J. W. Cooley (2011) “Simultaneous observation of peptide backbone lipid solvation and alpha-helical content by deep-UV resonance Raman spectroscopy” Chembiochem 12:2125-2128.

C. M. Halsey, J. Xiong, O. Oshokoya, S. Shinde, G. Ghirlanda, R. D. JiJi, and J. W. Cooley (2011) “Deep-UV resonance Raman analysis of the Rhodobacter capsulatus cytochrome bc1 complex reveals a potential marker for the transmembrane peptide backbone” Biochemistry 50:6531-6538.

J. W. Cooley (2010) “The transmission of a quinone binding signal through a transmembrane protein: a mechanistic proposal” Special issue of BBA Bioenergetics dedicated “quinone binding and catalysis” submitted Jan. 2010.

J. W. Cooley, D.W. Lee, E. A. Berry and F. Daldal (2009) “Across membrane communication between the Qo and Qi active sites of cytochrome bc1” Biochemistry 48: 1888-1899

J. W. Cooley, Nitschke, W. and D. Kramer (2008) “Mechanism of the cytochrome bc complexes" in The Purple Bateria, 2nd edition, Hunter ed. Elsevier Academic Press

D-W. Lee, Y. Ozturk, A. Osyczka, J. W. Cooley and F. Daldal (2008) “Cytochrome bc1-cy fusion complexes reveal the distance constraints for functional electron transfer between photosynthesis components” Journal of Biological Chemistry 283:13973-13982

D-W. Lee, Y. Ozturk, A. Mamedova, A. Osyczka, J. W. Cooley and F. Daldal (2006) “A functional hybrid between the cytochrome bc1 complex and its physiological membrane anchored acceptor cytochrome cy in Rhodobacter capsulatus” Biochimica et Biophysica Acta-Bioenergetics 1757:346-352

J. W. Cooley, T. Ohnishi, and F. Daldal (2005) “Binding dynamics at the quinone reduction (Qi) site influence the equilibrium interactions of the iron sulfur protein and hydroquinone oxidation (Qo) site of the cytochrome bc1 complex.” Biochemistry 44:10520-10532

M. K. Mathers, E. Darrouzet, M. Valkova-Valchanova, J. W. Cooley, M. T. McIntosh, F. Daldal and A. B. Vaidya (2005) “Uncovering the molecular mode of action of the antimalarial drug Atovaquone using a bacterial system.” Journal of Biological Chemistry 280:27458-27465

J. W. Cooley, A. Roberts, M. Bowman, D. Kramer, and F. Daldal (2004) “The raised midpoint potential of the [2Fe-2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S subunit.” Biochemistry 43:2217-2227

E. Darrouzet, J. W. Cooley, and F. Daldal (2004) “The cytochrome bc1 complex and its homologue the b6f complex: similarities and differences.” Photosynthesis Research 79:25-44

J. W. Cooley, E. Darrouzet, and F. Daldal (2004) “Bacterial hydroquinone: cyt c oxidoreductases: physiology, structure and function.” In: Respiration in Archaea and Bacteria D. Zannoni ed., Kluwer Academic Publishers.

J. W. Cooley, and W. F. J. Vermaas (2001) “Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp. PCC 6803: capacity comparisons and physiological function.” Journal of Bacteriology 183:4251-4258

C. Howitt, J. W. Cooley, J. Wiskich, and W. F. J. Vermaas (2001) A strain of Synechocystis sp. PCC 6803 without photosynthetic oxygen evolution and respiratory oxygen consumption: implication for the study of cyclic photosynthetic electron transport.” Planta 214:46-56

J. W. Cooley, C. Howitt, and W. F. J. Vermaas (2000) “ Succinate:quinol oxidoreductases in the cyanobacterium Synechocystis sp. PCC 6803: presence and function in metabolism and electron transport.” Journal of Bacteriology 182:714-722