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Curriculum Vitae Mark L Paddock, Ph.D

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Curriculum Vitae Mark L Paddock, Ph.D Curriculum Vitae Mark L Paddock, Ph.D. Department of Physics 0319, University of California, San Diego La Jolla, CA 92093-0319 Home: (858) 350-8984; Office: (858) 534-2504 E-mail: [email protected] Qualifications: ● Published 69 papers on research; 61 in the area of photosynthesis. ● Designed and implemented research projects on studies of proton transfer pathways, coupling of proton and electron transfer and quantum efficiency in the photosynthetic reaction center. ● Invited speaker to international and national meetings ● Supervised molecular biological technical research and graduate student work. Education: Ph.D. Physics (Biophysics), University of California, San Diego, La Jolla, California, 1991 Thesis Work: Characterization of Mutant Photosynthetic Reaction Centers from Rhodobacter sphaeroides: Investigation of Herbicide-Resistance and the Proton Transfer Pathway Advisors: Prof. Melvin Okamura, Prof. George Feher M.S. Physics, University of California, San Diego, La Jolla, California, 1984 B.S. Physics, Harvey Mudd College, Claremont, California, 1983 Research and Professional Experience at University of California, San Diego: 2005-present Project Scientist Implemented several photosynthetic research projects using site- directed mutagenesis, biochemical quinone substitution, EPR and ENDOR spectroscopy, X-ray crystallography in collaboration with Professors Melvin Okamura and George Feher. Implemented spectroscopic studies, prepared biochemical samples and made optical measurements. Supervised molecular biology technician and aided in supervising graduate research. 2002-present Lecturer in Summer Session Prepared lectures for Physics 2BL and Physics 2CL courses, supervised teaching assistants, coordinated with lab technician for experimental setups. 1999-2005 Associate Project Scientist Involved in projects using site-directed mutagenesis, biochemical quinone substitution, EPR spectroscopy, X-ray crystallography. 1993-1999 Assistant Project Scientist 1991-1993 Postdoctoral Research Physicist 1984-1991 Research Assistant 1983-1984, 1988 Teaching Assistant Research Interests: (1) Understanding coupling of proton and electron transfer, a basic biochemical step that is fundamental in both respiratory and photosynthetic energy conversion processes. (2) Investigations of the novel roles that FeS proteins play in regulation of stress responses that is relevant to both human health and agricultural crop production. Research/Scholarly Activties: Published 69 articles in peer reviewed journals including Proceedings of the National Academy of Sciences USA, Journal of American Chemical Society, Journal of Molecular Biology, Journal of Biological Chemistry and Biochemistry. Complete list available upon request. Attended international meetings presenting/co-authored 17 talks/posters in the last 3 years. Meetings include Biophysical Society (San Francisco, CA; Boston, MA; Long Beach, CA), Proton Transfer in Biology (Telluride, Colorado), Gordon Conference on Iron-Sulfur Enzymes (Manchester, NH), Protein Society meeting (San Diego, CA). Selected Publications (from 69 peer-reviewed publications) 1. Graige MS, Paddock ML, Feher G, Okamura MY. (1999) Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: implications for the mechanism of electron and proton transfer in proteins. Biochemistry 38, 11465-11473 2. Paddock ML, Graige MS, Feher G, Okamura MY. (1999) Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+. Proc Natl Acad Sci USA. 96, 6183-6188. 3. Axelrod HL, Abresch EC, Paddock ML, Okamura MY and Feher G. (2000) Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers. Proc Natl Acad Sci USA. 97, 1542-1547. 4. Paddock ML, Feher G and Okamura MY (2000) Identification of the proton pathway in bacterial reaction centers: replacement of Asp-M17 and Asp-L210 with asn reduces the proton transfer rate in the presence of Cd2+. Proc Natl Acad Sci USA. 97, 1548-1553 5. Ädelroth, P., Paddock, M.L., Sagle, L.B., Feher, G. and Okamura, M.Y. (2000) Identification of the Proton Pathway in Bacterial Reaction Centers: Metal Ion Binding Decreases the Uptake Rate of Both Protons Associated with Reduction of QB to QBH2 Share a Common Entry Point. Proc. Natl. Acad. Sci. 97, 13086-13091. 6. Paddock, M.L., Ädelroth, P., Chang, C., Abresch, E.C., Feher, G. and Okamura, M.Y. (2001) Identification of the Proton Pathway in Bacterial Reaction Centers: Cooperation between Asp-M17 and Asp-L210 Facilitates Proton Transfer to the Secondary Quinone (QB). Biochemistry, 40, 6893-6902. 7. Paddock, M.L., Ädelroth, P., Beatty, J.T., Feher, G. and Okamura, M.Y. (2002) Determination of Proton Transfer Rates by Chemical Rescue: Application to Bacterial Reaction Centers. Biochemistry, 41(50), 14716 – 14725. 8. Paddock, M.L., Sagle, L., Tehrani, A., Beatty, J.T., Feher, G. and Okamura, M.Y. (2003) Mechanism of Proton Transfer Inhibition by Cd2+ Binding to Bacterial Reaction Centers: Determination of the pKA of Functionally Important Histidine Residues. Biochemistry, 42, 9626–9632. 9. Paddock, M.L., Feher, G. and Okamura, M.Y. (2003) Proton Transfer Pathways and Mechanism in Bacterial Reaction Centers. Febs Lett. 555, 45-50. 10. Xu, Q., Axelrod, H.L., Abresch, E.C., Paddock, M.L., Okamura, M.Y. and Feher, G. (2004) X-Ray Structure Determination of Three Mutants of the Bacterial Photosynthetic Reaction Centers from Rhodobacter sphaeroides: Altered Proton Transfer Pathways. Structure 12, 703-715. 11. Paddock, M.L., Chang, C., Xu, Q., Abresch, E.C., Axelrod, H.L., Feher, G. and Okamura, M.Y. (2005) Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure. Biochemistry 44, 6920-6928. 12. Paddock, M. L., Flores, M., Isaacson, R., Chang, C., Abresch, E. C., Selvaduray, P. and Okamura, M. Y. (2006) Trapped conformational states of semiquinone (D(+center dot)Q(B)(-center dot)) formed by B-Branch electron transfer at low temperature in Rhodobacter sphaeroides reaction centers. Biochemistry 45, 14032-14042 13. Paddock, M. L., Isaacson, R. A., Abresch, E. C., and Okamura, M. Y. (2007) Light induced EPR spectra of reaction centers from Rhodobacter sphaeroides at 80K: Evidence for reduction of QB by B-branch electron transfer in native reaction centers, Appl Mag Reson 31, 1-15. 14. Wiley, S.E., Paddock, M.L., Abresch, E. C., Gross, L., van der Geer, P., Nechushtai, R., Murphy, A. N., Jennings, P.A. and Dixon, J.E. (2007) The outer mitochondrial membrane protein mitoneet contains a novel redox active 2Fe-2S cluster. J. Biol. Chem 282, 23745- 23749. 15. Paddock, M. L., Flores, M., Isaacson, R., Chang, C., Abresch, E. C. and Okamura, M. Y. (2007) ENDOR Spectroscopy Reveals Light Induced Movement of the H-Bond from Ser- - L223 upon Forming the Semiquinone (QB ) in Reaction Centers from Rhodobacter sphaeroides, Biochemistry 46, 8234 – 8243 16. Paddock, M.L., Wiley, S.E., Axelrod, H.L., Cohen, A. E., Roy, M., Abresch, E. C., Capraro, D., Murphy, A. N., Nechushtai, R., Dixon, J.E. and Jennings, P.A. (2007) MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone, Proc. Natl. Acad. Sci. USA 104, 14342-14347. 17. Abresch, E. C., Paddock, M. L., Villalobos, M., Chang, C. and Okamura, M. Y. (2008) Interaction between Cytochrome c2 and the Photosynthetic Reaction Center from Rhodobacter sphaeroides: Role of Interprotein Hydrogen Bonds in Binding and Electron Transfer.Biochemistry 47, 13318-13325. 18. Iwata, T. , Paddock, M. L., Okamura, M. Y. and Kandori, H. (2009) Identification of FTIR Bands Due to Internal Water Molecules around the Quinone Binding Sites in the Reaction Center from Rhodobacter sphaeroides. Biochemistry 48, 1220-1229. 19. Tirrell, T., Paddock, M. L., Conlan, A. R., Smoll, Jr., E. J., Nechushtai, R., Jennings, P. A. and Kim, J. E. (2009) Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of mitoNEET: Comparison to the (Cys)4 mutant and implications of the pH effects on the labile metal center. Biochemistry 48, 4747–4752. 20. Conlan, A. R., Axelrod, H. L., Cohen, A. E., Abresch, E. C., Zuris, J., Yee, D., Nechushtai, R., Jennings, P. A. and Paddock, M. L. (2009) Crystal Structure of Miner1 shows that the Protein Causitive in Wolfram Syndrome 2 Contains Redox Active 2Fe-2S clusters. J Mol Biol. 392, 143-153. 21. Paddock, M.L., Flores, M., Isaacson, R., Shepherd, J.N. and Okamura, M.Y. (2010) EPR and ENDOR investigation of rhodosemiquinone in bacterial reaction centers formed by B- branch electron transfer. Appl. Magn. Reson. 37, 39–48. 22. Dicus, Michelle M., Conlan, Andrea, Nechushtai, Rachel, Jennings, Patricia A., Paddock, Mark L., Britt, R. David and Stoll, Stefan (2010) The Binding of Histidine in the (Cys)3(His)1-coordinated [2Fe-2S] Cluster of Human mitoNEET. J. Am. Chem. Soc. 32, 2037-2049. 23. Zuris, J.A., Halim, D.A., Conlan, A.R., Abresch, E.C., Nechushtai, R., Paddock, M.L. and Jennings, P.A. (2010) Engineering the Redox Potential over a Wide Range within a New Class of FeS Proteins. J. Am. Chem. Soc. (Communication) 132, 13120-13122. Selected Invited Presentations: University of California, Riverside, California, Invited Speaker Biochemistry, June 2009 Gordon Conference on Iron-Sulfur Enzymes, New Hampshire, Invited Speaker, June 2008 Proton Transfer in Biology, Telluride, Colorado, Invited Speaker, July-August 2007 West Coast
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