个人简介
Kevin Redding received a B.A. in biochemistry from Rice University in 1987 and a Ph.D. degree in biochemistry from Stanford University in 1993, working with Robert Fuller. He was a National Science Foundation (NSF) Plant Biology Postdoctoral Fellow and a Human Frontiers in Science Postdoctoral Fellow and worked with Jean-David Rochaix at the University of Geneva. He started his academic career at the University of Alabama in 1998, received a DuPont Young Professor award and NSF CAREER award. After a one-year stint at the Institut de Biologie Physico-Chimique in Paris as a Fulbright Scholar, he joined ASU in 2008. His current research interests are in structure/function studies of photosynthetic reaction centers, re-engineering photosynthetic electron transfer, and fundamental processes in heliobacteria.
Education
Ph.D. Biochemistry, Stanford University 1993
B.A. Biochemistry, Rice University 1987
Positions
Positions: Arizona State University, Professor of Chem. & Biochem. (8/21/2014 – present)
Director of the Center for Bioenergy and Photosynthesis (1/1/2015 – present)
Arizona State University, Assoc. Prof. of Chem. & Biochem. (1/1/08 – 8/20/2014)
Fulbright Research Scholar & Chercheur associé (CNRS), Institut de Biologie PhysicoChimique, Paris (8/15/07–7/20/08)
University of Alabama, Associate Professor of Chemistry (8/16/04 – 12/30/07)
University of Alabama, Assistant Professor of Chemistry (8/16/98 – 8/15/04)
University of Geneva (Geneva, Switzerland), Maître-assistant in Plant Biol. Dept. (1998)
N.S.F. Plant Biology Postdoctoral Fellow (1995-1997)
Human Frontiers in Science Postdoctoral Fellow (1994)
研究领域
The Redding group works on the function of photochemical reaction centers, the key components in the energy conversion process of photosynthesis. As a model system, we are using Photosystem 1 (PS1), a multi-subunit membrane protein complex that uses the energy of absorbed photons to promote transmembrane electron transfer. The core of PS1 is a heterodimer of two homologous, integral membrane polypeptides, which form a framework holding the cofactors involved in electron transport.
1) Structure/function studies: One of the most interesting questions in biochemistry is "How does the protein environment affect the properties of bound molecules?" The phylloquinone cofactor embedded in PS1 is an excellent example. It is much more reducing when bound in PS1 than when isolated in organic solvent. Thus, the protein is able to "tune" the properties of the quinone so that it functions as a good intermediate in electron transfer. We are using site-directed mutagenesis to change amino acid residues that interact with the phylloquinone, and thus change its properties. Characterization of the mutants involves use of advanced techniques, such as electron paramagnetic resonance and kinetic spectroscopy.
2) Engineering electron transfer: The symmetric structure of PS1 includes two possible pathways of electron transfer. By changing amino acids around one quinone or the other, we have shown that both pathways can be used. We are altering the two quinone sites to see how the differences between them translate into different electron transfer rates. We hope to alter the sites enough to allow binding of alternate target molecules, which may lead to light-powered biomolecular devices capable of reductively destroying environmental pollutants, etc. We are also trying to see if we can control which pathway the electrons take by modify the environment near the electron donors.
3) Electron transfer processes in Heliobacteria: Our newest project involves engineering of the most primitive photosynthetic organism currently known. They use a homodimeric reaction center that is superficially similar to PS1 in several ways. The genome of Heliobacterium modesticaldum, the only thermophilic organism in this group, was recently determined in a collaboration between TGen and ASU . We have recently developed a transformation system for this organism, and are using it to delete key proteins involved in photosynthetic electron transfer and biosynthesis of cofactors. Long-term goals include: gaining insight into the evolution of asymmetric photosynthetic reaction centers, assessing alternative roles for quinones in this group of organisms, and optimizing their production of hydrogen.
近期论文
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Kanygin, A., Milrad, Y., Thummala, C, Reifschneider, K., Baker, P., Marco, P., Yacoby, I, Redding, K.E. Rewiring photosynthesis: a photosystem I-hydrogenase chimera that makes H-2 in vivo. Energy & Environmental Science 13 (9), 2903-2914 (2020).
Johnson, W.A., Redding, K.E. Reconstitution of the heliobacterial photochemical reaction center and cytochrome c(553) into a proteoliposome system. Photosynth. Res. 143 (3), 241-250 (2020).
Orf, G.S., Redding, K.E. Expression and purification of affinity-tagged variants of the photochemical reaction center from Heliobacterium modesticaldum. Photosynthesis Research. 142 (3) 335-348 (2019).
Baker, P.L., Orf, G.S., Kevershan, K., Pyne, M.E., Bicer, T., Redding, K.E. Using the Endogenous CRISPR-Cas System of Heliobacterium modesticaldum To Delete the Photochemical Reaction Center Core Subunit Gene. Applied and Environmental Microbiology. 85 (23) (2019).
Baker, P.L., Orf, G.S., Khan, Z., Espinoza, L., Leung, S., Kevershan, K., Redding, K.E., A Molecular Biology Tool Kit for the Phototrophic Firmicute Heliobacterium modesticaldum. Applied and Environmental Microbiology. 85 (19) (2019).
Kashey, T., D.D. Luu, J.B. Cowgill, P.L. Baker, K.E. Redding*. Light-driven quinone reduction in heliobacterial membranes. Photosynth. Res., in press (2018).
Marco, P., Kozuleva, M., Eilenberg, H., Mazor, Y., Gimeson, P., Kanygin, A., Redding, K., Weiner, I., Yacoby, I. Binding of ferredoxin to algal photosystem I involves a single binding site and is composed of two thermodynamically distinct events. Biochimica et Biophysica Acta-Bioenergetics. 1859 (4) 234-243 (2018).
Badshah SL, Sun J, Mula S, Gorka M, Baker P, Luthra R, Lin S, van der Est A, Golbeck JH, Redding KE. Mutations in algal and cyanobacterial Photosystem I that independently affect the yield of initial charge separation in the two electron transfer cofactor branches. Biochim Biophys Acta 1859:42-55 (2018).
Gisriel, C., I. Sarrou, B. Ferlez, J.H. Golbeck, K.E. Redding, R. Fromme. Structure of a symmetric photosynthetic reaction center-photosystem. Science 357:1021-1025 (2017).
Ferlez, B., Cowgill, J., Dong, W., Gisriel, C., Lin, S., Flores, M., Walters, K., Cetnar, D., Redding, K. E., and Golbeck, J. H. Thermodynamics of the Electron Acceptors in Heliobacterium modesticaldum: An Exemplar of an Early Homodimeric Type I Photosynthetic Reaction Center, Biochem. 55:2358-2370 (2016).
Ferlez B, Dong W, Siavashi R, Redding K, Hou HJ, Golbeck JH, van der Est A. The Effect of Bacteriochlorophyll g Oxidation on Energy and Electron Transfer in Reaction Centers from Heliobacterium modesticaldum. J Phys Chem B (2015).
McConnell, M.D., J. Sun, R. Siavashi, A.N. Webber, K.E. Redding, J.H. Golbeck, and A. van der Est. Species Dependent Alteration of Electron Transfer in Photosystem I. Biochim. Biophys. Acta Bioenergetics (2015).
Ort, D.R., S.S. Merchant, J. Alric, A. Barkan, R.E. Blankenship, R. Bock, R. Croce, M.R. Hanson, J.M. Hibberd, D.L. Lindstrom, S.P. Long, T.A. Moore, J. Moroney, K.K. Niyogi, M. Parry, P. Peralta-Yahya, R. Prince, K.E. Redding, M.H. Spalding, K. van Wijks, W.F.J. Vermaas, S. von Caemmerer, A.P.M. Weber, T. Yeates, J. Yuan, X. Zhu. Redesigning photosynthesis to sustainably meet global food and bioenergy demand. Proc. Natl. Acad. Sci. USA (2015).
Santabarbara, S., B. Bullock, F. Rappaport, K.E. Redding. Controlling electron transfer between the two cofactor chains of Photosystem I by the redox state of one of their components. Biophys. J (2015).
Yang, J.-H., Sarrou, I., Martin-Garcia, J.M., Zhang, S., Redding, K.E., Fromme, P. Purification and biochemical characterization of the ATP synthase from Heliobacterium modesticaldum. Protein Expression and Purification (2015).
Giera, W., S. Szewczyk, M.D. McConnell, J. Snellenburg, K.E. Redding, R. van Grondelle, K. Gibasiewicz. Excitation dynamics in Photosystem I from Chlamydomonas reinhardtii. Comparative studies of isolated complexes and whole cells. Biochem. Biophys. Acta Bioenergetics (2014).
K.E. Redding, I. Sarrou, F. Rappaport, S. Santabarbara, S. Lin, and K. Reifschneider. Modulation of the fluorescence yield in Heliobacterial cells by induction of charge recombination in the photosynthetic reaction center. Photosynthesis Research (2014).
Kashey, T., J.B. Cowgill, M.D. McConnell, M. Flores, K.E. Redding. Expression and characterization of cytochrome c553 from Heliobacterium modesticaldum. Photosynthesis Research (2014).
McConnell, M.D., D. Lowry, T.N. Rowan, K. van Dijk and K.E. Redding. Purification and photobiochemical profile of photosystem 1 from high-salt tolerant, oleaginous Chlorella (Trebouxiophycaea, Chlorophyta). Biochem Cell Biol (2014).
Reifschneider*, K.T., A. Kanygin, and K.E. Redding*. (2014). Expression of the [FeFe] hydrogenase in the chloroplast of Chlamydomonas reinhardtii. International Journal of Hydrogen Energy (2014).
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