Geoffrey Hind

Senior Biochemist

Brookhaven National Laboratory
Bldg. 463 - P.O. Box 5000
Upton, NY 11973-5000

Research Interests

Molecular mechanisms protect higher plants and algae against cellular damage during stress arising from excessive light collection by the photosynthetic antenna. Earlier studies showed that reversible phosphorylations of the light-harvesting protein complex of photosystem II (LHC-II) and the photosystem II reaction centers are driven by two distinct protein kinases, and regulate excitation energy distribution in low to moderate light intensity regimes. At higher intensities typical of the photoinhibition regime, LHC-II in thylakoid membranes and in detergent-isolated, two-dimensional crystals undergoes profound reorganization evidenced by loss of chirality. Scanning Transmission Electron Microscopy (STEM) analysis showed that hexagonal crystalline arrays of LHC-II are disrupted into polydisperse particles under these conditions, consistent with a proposed trimer-monomer transition in LHC-II. STEM also revealed a novel microcrystalline form of lipid-depleted LHC-II which has strong chirality but is structurally resistant to intense light. Its unit cell is rhombic, and the two-dimensional crystals have uniquely high mean mass per unit area. Current experiments explore the organization of trimers in these microcrystals.

Selected Publications

• Dunn J.J., McCorkle S.R., Praissman L.A., Hind G., van der Lelie D., Bahou W.F., Gnatenko D.V. and Krause M.K.
  Genomic Signature Tags (GSTs): A system for profiling genomic DNA.
  Genome Research, 12:1756-65 (2002).   PubMed   Full Text
• Race H.L., Forsberg J., Hind G. and Allen J.F.
  Photosystem II-associated protein kinase phosphorylates a novel 6.3 kDa protein which subsequently dissociates from photosystem II core complexes.
  In: Photosynthesis: Mechanisms and Effects, Proceedings of XIth International Congress on Photosynthesis (G. Garab, edt.), Dordrecht: Kluwer Academic Publishers, 3: 1859-1863 (1998).
• Race H.L. and Hind G.
  Minor constituents of photosystem II core complexes: Possible regulators of photosystem II protein kinase.
  Arch Biochem Biophys., 345:355-357 (1997).   PubMed
• Race H.L. and Hind G.
  A protein kinase in the core of photosystem II.
  Biochemistry, 35:13006-13010 (1996).   PubMed   Full Text
  See also article in the Brookhaven Bulletin (1996: Vol.50 No.46).
• Hind G., Marshak D.R. and Coughlan S.J.
  Spinach thylakoid polyphenol oxidase: cloning, characterization, and relation to a putative protein kinase.
  Biochemistry, 34:8157-8164 (1995).   PubMed
• France L.L., Kieleczawa J., Dunn J.J., Luft B.J., Hind G., and Sutherland J.C.
  Evidence of an alpha-helical epitope on outer surface protein A from the Lyme disease spirochete, Borrelia burgdorferi: an application of steady-state and time-resolved fluorescence quenching techniques.
  Biochim. Biophys. Acta, 1202:287-296 (1993).   PubMed
• Kieleczawa J., Coughlan S.J. and Hind G.
  Isolation and characterization of an alkaline phosphatase from pea thylakoids.
  Plant Physiol., 99:1029-1036 (1992).

Last Modified: April 17, 2009
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One of ten national laboratories overseen and primarily funded by the Office of Science of the U.S. Department of Energy (DOE), Brookhaven National Laboratory conducts research in the physical, biomedical, and environmental sciences, as well as in energy technologies and national security. Brookhaven Lab also builds and operates major scientific facilities available to university, industry and government researchers. Brookhaven is operated and managed for DOE's Office of Science by Brookhaven Science Associates, a limited-liability company founded by the Research Foundation for the State University of New York on behalf of Stony Brook University, the largest academic user of Laboratory facilities, and Battelle, a nonprofit, applied science and technology organization.

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