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Donatas Zigmantas. Portrait.

Donatas Zigmantas

Professor

Donatas Zigmantas. Portrait.

Carotenoid S(1) state in a recombinant light-harvesting complex of Photosystem II.

Author

  • Tomas Polivka
  • Donatas Zigmantas
  • Villy Sundström
  • Elena Formaggio
  • Gianfelice Cinque
  • Roberto Bassi

Summary, in English

The carotenoid species lutein, violaxanthin, and zeaxanthin are crucial in the xanthophyll-dependent nonphotochemical quenching occurring in photosynthetic systems of higher plants, since they are involved in dissipation of excess energy and thus protect the photosynthetic machinery from irreversible inhibition. Nonetheless, important properties of the xanthophyll cycle carotenoids, such as the energy of their S(1) electronic states, are difficult to study and were only recently determined in organic solvents [Polívka, T. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 4914. Frank, H. A. (2000) Biochemistry 39, 2831]. In the present study, we have determined the S(1) energies of three carotenoid species, violaxanthin, lutein, and zeaxanthin, in their LHCII (peripheral light-harvesting complex of photosystem II) protein environment by constructing recombinant Lhcb1 (Lhc = light-harvesting complex) proteins containing single carotenoid species. Within experimental error the S(1) energy is the same for all three carotenoids in the monomeric LHCII, 13,900 +/- 300 cm(-1) (720 +/- 15 nm), thus well below the Q(y)() transitions of chlorophylls. In addition, we have found that, although the S(1) lifetimes of violaxanthin, lutein, and zeaxanthin differ substantially in solution, when incorporated into the LHCII protein, their S(1) states have in fact the same lifetime of about 11 ps. Despite the similar spectroscopic properties of the carotenoids bound to the LHCII, we observed a maximal fluorescence quenching when zeaxanthin was present in the LHCII complex. On the basis of these observations, we suggest that, rather than different photochemical properties of individual carotenoid species, changes in the protein conformation induced by binding of carotenoids with distinct molecular structures are involved in the quenching phenomena associated with Lhc proteins.

Department/s

  • Chemical Physics

Publishing year

2002

Language

English

Pages

439-450

Publication/Series

Biochemistry

Volume

41

Issue

2

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Biological Sciences

Keywords

  • Kinetics
  • Light
  • Lutein : chemistry
  • Photosynthetic Reaction Center Plant
  • Recombinant Proteins : chemistry : metabolism
  • Spectrometry Fluorescence
  • Support Non-U.S. Gov't
  • Spectrophotometry
  • beta Carotene : analogs & derivatives : chemistry
  • Time Factors
  • Electrophysiology
  • Carotenoids : chemistry

Status

Published

ISBN/ISSN/Other

  • ISSN: 0006-2960