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The Structural Basis of Biological Energy Generation pp 21–37Cite as

Structure and Functional Heterogeneity of Fucoxanthin-Chlorophyll Proteins in Diatoms

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

Summary

Fucoxanthin-chlorophyll proteins (FCPs) of diatoms are divided into three groups, the main light harvesting antennas Lhcf, the photosystem I-specific Lhcr, and Lhcx involved in photoprotection. All are closely related to higher plant light harvesting complexes (LHCs) when comparing sequences, albeit smaller and more hydrophobic. However, pigmentation differs from higher plant LHCs with around eight chlorophyll a, two chlorophyll c and six fucoxanthin per monomer. Fucoxanthin, with a carbonyl moiety conjugated to the polyene backbone, undergoes extreme bathochromic shifts upon protein binding, dividing the different fucoxanthins into more red, green and blue absorbing ones. Excitation energy transfer is extremely efficient, either directly from chlorophyll c to chlorophyll a or from fucoxanthin to chlorophyll a involving the S1/ICT state of fucoxanthin. Most Lhcf assemble into trimers, whereby only in centric diatoms Lhcx was found in trimers as well, and specific oligomeric FCP complexes are present. Whereas the arrangement of FCPs around the photosystems is largely unknown, spectroscopic measurements together with homology considerations allow for a first rough model of the pigment arrangement in trimeric and oligomeric FCP complexes. Blue fucoxanthin is bound analogously to lutein in LHCII, surrounded by the same four chlorophyll a, since binding sites are conserved. Additionally, chlorophyll a can be found in a604, a614, b605 and a611, although binding of the latter has to be different due to the lack of long wavelength absorption in FCPs. Chlorophyll c is most probably bound in b609 and a613. The red fucoxanthin cluster around helix 2, which has less sequence homology to LHCII. The green fucoxanthins are most probably located around the violaxanthin and b601 binding sites of LHCII, whereby the former is probably a mixed site for fucoxanthins and diadinoxanthin/diatoxanthin.

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Abbreviations

Chl:

– Chlorophyll;

Dd:

– Diadinoxanthin;

Dt:

– Diatoxanthin;

FCP:

– Fucoxanthin-chlorophyll protein;

Fx:

– Fucoxanthin;

LHC:

– Light-harvesting complex;

NPQ:

– Non-photochemical quenching;

PS:

– Photosystem

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Acknowledgments

CB would like to express her extreme thankfulness to her present and former group members, colleagues and collaborators, without whom the vast increase in our knowledge about FCP structure and function during the last years would not have been possible. CB and KG gratefully acknowledge continuous support by the Deutsche Forschungsgemeinschaft (Bu812: grants 4–8) and the European Union (MRTN-CT-2003-505069 “Intro2”; MC-ITN-2009-238017 “Harvest”).

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  1. Institute of Molecular Biosciences, Goethe Universität Frankfurt, D-60438, Frankfurt, Germany

    Kathi Gundermann & Claudia Büchel

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  1. Kathi Gundermann
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Correspondence to Claudia Büchel .

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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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Gundermann, K., Büchel, C. (2014). Structure and Functional Heterogeneity of Fucoxanthin-Chlorophyll Proteins in Diatoms. 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_2

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