Unknown

Dataset Information

0

A Protein Environment-Modulated Energy Dissipation Channel in LHCII Antenna Complex.


ABSTRACT: The major light-harvesting complex of photosystem II (LHCII) is the main contributor to sunlight energy harvesting in plants. The flexible design of LHCII underlies a photoprotective mechanism whereby this complex switches to a dissipative state in response to high light stress, allowing the rapid dissipation of excess excitation energy (non-photochemical quenching, NPQ). In this work, we locked single LHCII trimers in a quenched conformation after immobilization of the complexes in polyacrylamide gels to impede protein interactions. A comparison of their pigment excited-state dynamics with quenched LHCII aggregates in buffer revealed the presence of a new spectral band at 515 nm arising after chlorophyll excitation. This is suggested to be the signature of a carotenoid excited state, linked to the quenching of chlorophyll singlet excited states. Our data highlight the marked sensitivity of pigment excited-state dynamics in LHCII to structural changes induced by the environment.

SUBMITTER: Saccon F 

PROVIDER: S-EPMC7452274 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

A Protein Environment-Modulated Energy Dissipation Channel in LHCII Antenna Complex.

Saccon Francesco F   Durchan Milan M   Bína David D   Duffy Christopher D P CDP   Ruban Alexander V AV   Polívka Tomáš T  

iScience 20200802 9


The major light-harvesting complex of photosystem II (LHCII) is the main contributor to sunlight energy harvesting in plants. The flexible design of LHCII underlies a photoprotective mechanism whereby this complex switches to a dissipative state in response to high light stress, allowing the rapid dissipation of excess excitation energy (non-photochemical quenching, NPQ). In this work, we locked single LHCII trimers in a quenched conformation after immobilization of the complexes in polyacrylami  ...[more]

Similar Datasets

| S-EPMC2749134 | biostudies-literature
| S-EPMC9615032 | biostudies-literature
| S-EPMC4616226 | biostudies-literature
2018-09-20 | GSE104797 | GEO
| S-EPMC3351333 | biostudies-literature
| S-EPMC3195717 | biostudies-literature
| S-EPMC2662029 | biostudies-literature
2021-01-01 | GSE142424 | GEO
| S-EPMC7712781 | biostudies-literature
| S-EPMC1769499 | biostudies-literature