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Structure-Function Relationship in Peridinin-Chlorophyll Proteins

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The Structural Basis of Biological Energy Generation

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 39))

Summary

An important component of the photosynthetic apparatus is a light-harvesting system that captures light energy and transfers it efficiently to the reaction center. Depending on environmental conditions, photosynthetic antennas have adopted various strategies for this function. The water soluble antenna complex of dinoflagellates, peridinin–chlorophyll a protein (PCP), represents a unique light-harvesting strategy because, unlike other antenna systems which have a preponderance of chlorophyll, the carotenoid peridinin serves in PCP as the major light-harvesting pigment. The key structural feature of peridinin is a conjugated carbonyl group which makes the spectroscopic properties of peridinin very sensitive to its local environment. This property is a crucial factor for maintaining the high efficiency of energy transfer between peridinin and Chl a in PCP. PCP is also amenable to site-directed mutagenesis and reconstitution with different pigments, allowing to study effects of both pigment and amino acid exchange on energy transfer pathways within the complex. Since high resolution structures of native, reconstituted and mutated PCP complexes are now available, this knowledge provides an ideal platform to relate structural motifs to energy transfer pathways and efficiencies in PCP. This Chapter summarizes results of structural and spectroscopic investigations of PCP and related proteins, emphasizing the specific light-harvesting strategy developed by dinoflagellates.

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Abbreviations

BChl:

– Bacteriochlorophyll;

CD:

– Circular dichroism;

Chl:

– Chlorophyll;

ENDOR:

– Electron nuclear double resonance;

EPR:

– Electron paramagnetic resonance;

FCP:

– Fucoxanthin chlorophyll protein;

HSPCP:

– High salt PCP;

ICT:

– Intramolecular charge transfer;

LD:

– Linear dichroism;

LHC:

– Light harvesting complex;

MFPCP:

– Main form PCP used when needed to distinguish from other forms;

MNDO-PSCDI:

– Modified neglect of differential overlap with partial single and double configuration interaction;

NIR:

– Near infra red;

PCP:

– Peridinin chlorophyll protein;

Per:

– Peridinin;

RFPCP:

– Refolded PCP construct equivalent to the N-terminal domain of MFPCP;

VIS:

– Visible

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Acknowledgment

The authors thank Roger Hiller and Harry Frank for many years of collaboration on research described in this chapter. Harry Frank is greatly acknowledged for providing data for Fig. 3.12. TP thanks the Czech Science Foundation (P205/11/1164) for financial support. EH acknowledges support by the collaborative research center SFB480 (project C6) of the Deutsche Forschungsgemeinschaft.

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Authors and Affiliations

  1. Faculty of Science, Department of Physics and Biophysics, University of South Bohemia, 370-05, České Budějovice, Czech Republic

    Tomáš Polívka

  2. Faculty of Biology and Biotechnology, Department of Biophysics, Ruhr-University Bochum, D-44780, Bochum, Germany

    Eckhard Hofmann

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Correspondence to Tomáš Polívka .

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  1. Department of Biotechnology, Norwegian University of Science and Technology, Trondheim, Sør-Trøndelag Fylke, Norway

    Martin F. Hohmann-Marriott

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Polívka, T., Hofmann, E. (2014). Structure-Function Relationship in Peridinin-Chlorophyll Proteins. In: Hohmann-Marriott, M. (eds) The Structural Basis of Biological Energy Generation. Advances in Photosynthesis and Respiration, vol 39. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-8742-0_3

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