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Chapter 16 Folding and Pigment Binding of Light-Harvesting Chlorophyll a/b Protein (LHCIIb)

  • Chapter
The Chloroplast

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 31))

Summary

The major light-harvesting chlorophyll a/b protein (LHCIIb) is one of the most abundant proteins of the chloroplast in green plants. It contains roughly half of the chlorophylls involved in photosynthesis, and exhibits an unusual ability to self-organize in vitro. Simply mixing the apoprotein, native or recombinant, with its pigments, chlorophyll a, chlorophyll b, and xanthophylls, in detergent solution, suffices to trigger protein folding and the assembly of about 18 pigments in their correct binding sites. A study of the mechanism of this self-organization seems worthwhile since (1) our knowledge about membrane protein folding is scarce compared to what we know about the folding of water-soluble proteins, (2) the mechanism of LHCIIb formation in vitro may give useful clues about the so-far unknown pathway of its assembly in the chloroplast, and (3) a thorough understanding of the process may facilitate the application of recombinant LHCIIb in hybrid constructs such as photovoltaic devices or the construction of potentially useful proteins or other polymers that spontaneously bind other dyes at a similarly high density.

During the assembly of recombinant LHCIIb, the formation of protein secondary structure is triggered by the binding of pigments. Chlorophylls are bound in two apparent kinetic phases. A faster one in the range of tens of seconds reflects the binding of chlorophyll a along with xanthophylls. During the slower step in the range of minutes, mostly chlorophyll b is bound. The intermediate complex lacking chlorophyll b is unstable and susceptible to proteases. The resulting two-step model of LHCIIb formation is able to explain why LHCIIb in vivo exhibits an apparently constant chlorophyll a:b ratio although several binding sites have been found to be accessible to both of the two chlorophylls in vitro and in plants over-producing chlorophyll b. Time-resolved electron paramagnetic resonance (EPR) techniques have been established to assess protein folding beyond secondary structure formation during LHCIIb assembly, and first results of EPR-monitored kinetics are shown.

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Abbreviations

CAO:

– chlorophyllide a oxygenase

CD:

– circular dichroism

Chl:

– chlorophyll

cpSRP:

– chloroplast signal recognition particle

EPR:

– electron paramagnetic resonance

LHCI, LHCII:

– light-harvesting Chl a/b complex of PSI and PSII, respectively

LHCIIb:

– major subunit of LHCII with apoproteins Lhcb1-3

NPQ:

– non-photochemical quenching

PSI, PSII:

– photosystems I and II, respectively

s:

– seconds

SDS:

– sodium dodecylsulfate

τ1, τ2:

– reaction times 1,2 = inverted rate constants k1, k2 in kinetic analyses

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Acknowledgment

Work in the author’s laboratory has been funded by the Deutsche Forschungsgemeinschaft (Pa 324/3-4, SFB 625 TP B10).

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Authors and Affiliations

  1. Institut für Allgemeine Botanik, Universität Mainz, Müllerweg 6, D-55099, Mainz, Germany

    Harald Paulsen & Christoph Dockter

  2. Max-Planck-Institut für Polymerforschung, Ackermannweg 10, D-55128, Mainz, Germany

    Aleksei Volkov

  3. Institut für Physikalische Chemie, Universität Konstanz, 78475, Konstanz, Germany

    Gunnar Jeschke

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  1. Harald Paulsen
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  2. Christoph Dockter
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  3. Aleksei Volkov
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  4. Gunnar Jeschke
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Correspondence to Harald Paulsen .

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Editors and Affiliations

  1. Rebeiz Foundation for Basic Research, Champaign, USA

    Constantin A. Rebeiz

  2. Michigan State University, East Lansing, USA

    Christoph Benning

  3. University of Illinois at Urbana-Champaign, Urbana, USA

    Hans J. Bohnert

  4. Central Florida University, Orlando, USA

    Henry Daniell

  5. Arizona State University, Tempe, USA

    J. Kenneth Hoober

  6. University of Karlsruhe, Germany

    Hartmut K. Lichtenthaler

  7. University of Illinois at Urbana-Champaign, Urbana, USA

    Archie R. Portis

  8. Jawaharlal Nehru University, New Delhi, India

    Baishnab C. Tripathy

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Paulsen, H., Dockter, C., Volkov, A., Jeschke, G. (2010). Chapter 16 Folding and Pigment Binding of Light-Harvesting Chlorophyll a/b Protein (LHCIIb). In: Rebeiz, C.A., et al. The Chloroplast. Advances in Photosynthesis and Respiration, vol 31. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-8531-3_16

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