Light-harvesting complexes of green plants explained

The light-harvesting complex (or antenna complex; LH or LHC) is an array of protein and chlorophyll molecules embedded in the thylakoid membrane of plants and cyanobacteria, which transfer light energy to one chlorophyll a molecule at the reaction center of a photosystem.

The antenna pigments are predominantly chlorophyll b, xanthophylls, and carotenes. Chlorophyll a is known as the core pigment. Their absorption spectra are non-overlapping and broaden the range of light that can be absorbed in photosynthesis. The carotenoids have another role as an antioxidant to prevent photo-oxidative damage of chlorophyll molecules. Each antenna complex has between 250 and 400 pigment molecules and the energy they absorb is shuttled by resonance energy transfer to a specialized chlorophyll-protein complex known as the reaction center of each photosystem.[1] The reaction center initiates a complex series of chemical reactions that capture energy in the form of chemical bonds.

For photosystem II, when either of the two chlorophyll a molecules at the reaction center absorb energy, an electron is excited and transferred to an electron acceptor molecule, pheophytin, leaving the chlorophyll a in an oxidized state. The oxidised chlorophyll a replaces the electrons by photolysis that involves the oxidation of water molecules to oxygen, protons and electrons.

The N-terminus of the chlorophyll a-b binding protein extends into the stroma where it is involved with adhesion of granal membranes and photo-regulated by reversible phosphorylation of its threonine residues.[2] Both these processes are believed to mediate the distribution of excitation energy between photosystems I and II.

This family also includes the photosystem II protein PsbS, which plays a role in energy-dependent quenching that increases thermal dissipation of excess absorbed light energy in the photosystem.[3]

LH 1

Light-harvesting complex I is permanently bound to photosystem I via the plant-specific subunit PsaG. It is made up of four proteins: Lhca1, Lhca2, Lhca3, and Lhca4, all of which belong to the LHC or chlorophyll a/b-binding family. The LHC wraps around the PS1 reaction core.[4]

LH 2

The LH 2 is usually bound to photosystem II, but it can undock and bind PS I instead depending on light conditions.[4] This behavior is controlled by reversible phosphorylation. This reaction represents a system for balancing the excitation energy between the two photosystems.[5]

References

See also

Notes and References

  1. Book: Biochemistry 4th Ed.. limited. Voet D, Voet JG . Wiley. 2011. 978-0470-57095-1. USA. 906.
  2. Yang DH, Paulsen H, Andersson B . The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis . FEBS Letters . 466 . 2–3 . 385–8 . January 2000 . 10682866 . 10.1016/S0014-5793(00)01107-8 . 19716587 .
  3. Li XP, Gilmore AM, Caffarri S, Bassi R, Golan T, Kramer D, Niyogi KK . Regulation of photosynthetic light harvesting involves intrathylakoid lumen pH sensing by the PsbS protein . The Journal of Biological Chemistry . 279 . 22 . 22866–74 . May 2004 . 15033974 . 10.1074/jbc.M402461200 . free .
  4. Book: Grotjohann I, Fromme P . Encyclopedia of biological chemistry . London . 978-0-12-378630-2 . Second . Photosystem I. 2013 . 503–507 . 10.1016/B978-0-12-378630-2.00287-5.
  5. Liu XD, Shen YG . NaCl-induced phosphorylation of light harvesting chlorophyll a/b proteins in thylakoid membranes from the halotolerant green alga, Dunaliella salina . FEBS Letters . 569 . 1–3 . 337–40 . July 2004 . 15225658 . 10.1016/j.febslet.2004.05.065 . 23367090 .