Engineering a pH-regulated switch in the major light-harvesting complex of plants (LHCII): proof of principle

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Under excess light, photosynthetic organisms employ feedback mechanisms to avoid photodamage. Photoprotection is triggered by acidification of the lumen of the photosynthetic membrane following saturation of the metabolic activity. A low pH triggers thermal dissipation of excess absorbed energy by the light-harvesting complexes (LHCs). LHCs are not able to sense pH variations, and their switch to a dissipative mode depends on stress-related proteins and allosteric cofactors. In green algae the trigger is the pigment–protein complex LHCSR3. Its C-terminus is responsible for a pH-driven conformational change from a light-harvesting to a quenched state. Here, we show that by replacing the C-terminus of the main LHC of plants with that of LHCSR3, it is possible to regulate its excited-state lifetime solely via protonation, demonstrating that the protein template of LHCs can be modified to activate reversible quenching mechanisms independent of external cofactors and triggers.
Original languageEnglish
Pages (from-to)12531-12535
JournalJournal of Physical Chemistry B
Volume120
Issue number49
DOIs
Publication statusPublished - 12 Nov 2016

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switches
Switches
engineering
actuators
Photosynthetic membranes
proteins
Proteins
lumens
Acidification
Protonation
algae
Algae
organisms
Excited states
Quenching
templates
dissipation
quenching
membranes
saturation

Keywords

  • LHCII
  • LHCSR
  • QUENCHING
  • PH REGULATION
  • LIGHT-HARVESTING
  • PHOTOPROTECTION
  • Mutation

Cite this

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title = "Engineering a pH-regulated switch in the major light-harvesting complex of plants (LHCII): proof of principle",
abstract = "Under excess light, photosynthetic organisms employ feedback mechanisms to avoid photodamage. Photoprotection is triggered by acidification of the lumen of the photosynthetic membrane following saturation of the metabolic activity. A low pH triggers thermal dissipation of excess absorbed energy by the light-harvesting complexes (LHCs). LHCs are not able to sense pH variations, and their switch to a dissipative mode depends on stress-related proteins and allosteric cofactors. In green algae the trigger is the pigment–protein complex LHCSR3. Its C-terminus is responsible for a pH-driven conformational change from a light-harvesting to a quenched state. Here, we show that by replacing the C-terminus of the main LHC of plants with that of LHCSR3, it is possible to regulate its excited-state lifetime solely via protonation, demonstrating that the protein template of LHCs can be modified to activate reversible quenching mechanisms independent of external cofactors and triggers.",
keywords = "LHCII, LHCSR, QUENCHING, PH REGULATION, LIGHT-HARVESTING, PHOTOPROTECTION, Mutation",
author = "N. Liguori and A. Natali and Roberta Croce",
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Engineering a pH-regulated switch in the major light-harvesting complex of plants (LHCII): proof of principle. / Liguori, N.; Natali, A.; Croce, Roberta.

In: Journal of Physical Chemistry B, Vol. 120, No. 49, 12.11.2016, p. 12531-12535.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Engineering a pH-regulated switch in the major light-harvesting complex of plants (LHCII): proof of principle

AU - Liguori, N.

AU - Natali, A.

AU - Croce, Roberta

PY - 2016/11/12

Y1 - 2016/11/12

N2 - Under excess light, photosynthetic organisms employ feedback mechanisms to avoid photodamage. Photoprotection is triggered by acidification of the lumen of the photosynthetic membrane following saturation of the metabolic activity. A low pH triggers thermal dissipation of excess absorbed energy by the light-harvesting complexes (LHCs). LHCs are not able to sense pH variations, and their switch to a dissipative mode depends on stress-related proteins and allosteric cofactors. In green algae the trigger is the pigment–protein complex LHCSR3. Its C-terminus is responsible for a pH-driven conformational change from a light-harvesting to a quenched state. Here, we show that by replacing the C-terminus of the main LHC of plants with that of LHCSR3, it is possible to regulate its excited-state lifetime solely via protonation, demonstrating that the protein template of LHCs can be modified to activate reversible quenching mechanisms independent of external cofactors and triggers.

AB - Under excess light, photosynthetic organisms employ feedback mechanisms to avoid photodamage. Photoprotection is triggered by acidification of the lumen of the photosynthetic membrane following saturation of the metabolic activity. A low pH triggers thermal dissipation of excess absorbed energy by the light-harvesting complexes (LHCs). LHCs are not able to sense pH variations, and their switch to a dissipative mode depends on stress-related proteins and allosteric cofactors. In green algae the trigger is the pigment–protein complex LHCSR3. Its C-terminus is responsible for a pH-driven conformational change from a light-harvesting to a quenched state. Here, we show that by replacing the C-terminus of the main LHC of plants with that of LHCSR3, it is possible to regulate its excited-state lifetime solely via protonation, demonstrating that the protein template of LHCs can be modified to activate reversible quenching mechanisms independent of external cofactors and triggers.

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KW - LHCSR

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KW - LIGHT-HARVESTING

KW - PHOTOPROTECTION

KW - Mutation

U2 - 10.1021/acs.jpcb.6b11541

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