Cu+ Contributes to the Orange Carotenoid Protein-Related Phycobilisome Fluorescence Quenching and Photoprotection in Cyanobacteria.

  title={Cu+ Contributes to the Orange Carotenoid Protein-Related Phycobilisome Fluorescence Quenching and Photoprotection in Cyanobacteria.},
  author={Wenjing Lou and Benjamin M. Wolf and Robert Eugene Blankenship and Haijun Liu},
Photosynthesis starts with absorption of light energy by using light-harvesting antenna complexes (LHCs). Overexcitation of LHCs and subsequent photosystems, however, is damaging and can be lethal. The orange carotenoid protein (OCP) protects most cyanobacteria from photodamage by dissipating excessive excitation energy harvested by phycobilisomes (PBS, LHCs) as heat. OCP has two states: the orange, inactive OCP (OCPO) and the red, active OCP (OCPR), with the latter able to bind PBS at a ratio… 

Changing Color for Photoprotection: The Orange Carotenoid Protein.

Probing heavy metal binding to phycobiliproteins

Monitoring the binding equilibria and metal‐binding stoichiometry reveals the mechanisms by which metal ions can modulate phycobiliproteins properties which can be used as a basis for the future design of metal‐related phyCobiliprotein applications.

Specific Features of Technogenic Pollutants Impact on Photosynthetic Activity of Unicellular Cyanobacteria

Abstract The effect of heavy-metal ions (Cd 2+ , Cr 6+ , and Cu 2+ ) on cyanobacteria sp. Microcystis and sp. Synechocystis has been studied. Since heavy metals impact causes blocking of light-energy

Prospects of fluorescence methods application for monitoring of cyanobacterial cultures in biotechnology

  • N. GrigoryevaA. A. Liss
  • Biology, Engineering
    Abstract book of the 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology" PLAMIC2020
  • 2020
On-line monitoring of cyanobacterial cultures using fluorescence spectroscopy for permanent control of growth rate, physiological state and algological purity should be controled permanently.

The role of fluorescence methods in environmental monitoring of cyanobacteria in aquatic systems

. In this article the main advantages of fluorescence spectroscopy in the environmental monitoring of cyanobacteria are pointed out. Several widely used environmental monitoring techniques are



Photoactivation and relaxation studies on the cyanobacterial orange carotenoid protein in the presence of copper ion

The effects and mechanisms of copper on cyanobacteria NPQ, photoactivation and relaxation of OCP in the presence of copper were examined and Native polyacrylamide gel electrophoresis (PAGE) analysis result indicates the heterogeneous population of Cu2+-locked OCPr.

Molecular mechanism of photoactivation and structural location of the cyanobacterial orange carotenoid protein.

An investigation on the OCP photoactivation from the cyanobacterium Synechocystis sp.

A Soluble Carotenoid Protein Involved in Phycobilisome-Related Energy Dissipation in Cyanobacteria

It is demonstrated that this photoprotective mechanism, characterized by blue light–induced fluorescence quenching, is indeed phycobilisome-related and that a soluble carotenoid binding protein, ORANGE CAROTENOID PROTEIN (OCP), encoded by the slr1963 gene in Synechocystis PCC 6803, plays an essential role in this process.

In Vitro Reconstitution of the Cyanobacterial Photoprotective Mechanism Mediated by the Orange Carotenoid Protein in Synechocystis PCC 6803[C][W]

In the cyanobacterial photoprotective mechanism, one red-activated Orange Carotenoid Protein binds to the core of the phycobilisome and quenches all its fluorescence, and protocols to overcome the effect of high phosphate concentrations are developed.

Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria

It is proposed that in vivo, FRP plays a key role in removing the red OCP from the phycobilisome and in the conversion of the free red O CP to the orange inactive form.

The Orange Carotenoid Protein: a blue-green light photoactive protein.

  • D. KirilovskyC. Kerfeld
  • Chemistry
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2013
In the last decade, in vivo and in vitro mechanistic studies combined with structural and genomic data resulted in both the discovery and a detailed picture of the function of the OCP and OCP-mediated photoprotection.

The photophysics of the orange carotenoid protein, a light-powered molecular switch.

OCP functions as a light-powered molecular switch that modulates its spectroscopic properties as a response to specific changes in light environment and is proposed as a mechanism wherein the red state of OCP echinenone acts as an energy dissipator via its charge transfer state.

OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria

Protein engineering, disulfide trapping and structural analyses are combined to provide mechanistic insights into the transient OCP-FRP interaction and may inspire the design of optically triggered systems transducing light signals into protein–protein interactions.

Single-molecule trapping and spectroscopy reveals photophysical heterogeneity of phycobilisomes quenched by Orange Carotenoid Protein

Photon-by-photon Monte Carlo simulations of exciton transfer through the phycobilisome suggest that the observed quenched states are kinetically consistent with either two or one bound OCPs, respectively, underscoring an additional mechanism for excitation control in this key photosynthetic unit.