Phycocyanin: One Complex, Two States, Two Functions

Gwizdala, Michal; Krüger, Tjaart P. J.; Wahadoszamen,; Gruber, J. Michael; Grondelle, Rienk van

doi:10.1021/acs.jpclett.8b00621

Cited by 31 publications

(40 citation statements)

References 39 publications

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“…Conformational changes in the phycobilins themselves may result in an improvement to some extent. Such changes were recently shown in vitro in phycocyanin [43]. It is possible that phycoerythrin has a similar switching mechanism.…”

Section: Discussionmentioning

confidence: 63%

Marine cyanobacteria tune energy transfer efficiency in their light‐harvesting antennae by modifying pigment coupling

et al. 2020

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Photosynthetic light harvesting is the first step in harnessing sunlight toward biological productivity. To operate efficiently under a broad and dynamic range of environmental conditions, organisms must tune the harvesting process according to the available irradiance. The marine cyanobacteria Synechococcus WH8102 species is well‐adapted to vertical mixing of the water column. By studying its responses to different light regimes, we identify a new photo‐acclimation strategy. Under low light, the phycobilisome (PBS) is bigger, with extended rods, increasing the absorption cross‐section. In contrast to what was reported in vascular plants and predicted by Forster resonance energy transfer (FRET) calculations, these longer rods transfer energy faster than in the phycobilisomes of cells acclimated to a higher light intensity. Comparison of cultures grown under different blue light intensities, using fluorescence lifetime and emission spectra dependence on temperature at the range of 4–200 K in vivo, indicates that the improved transfer arises from enhanced energetic coupling between the antenna rods' pigments. We suggest two physical models according to which the enhanced coupling strength results either from additional coupled pathways formed by rearranging rod packing or from the coupling becoming non‐classical. In both cases, the energy transfer would be more efficient than standard one‐dimensional FRET process. These findings suggest that coupling control can be a major factor in photosynthetic antenna acclimation to different light conditions.

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Section: Discussionmentioning

confidence: 63%

Marine cyanobacteria tune energy transfer efficiency in their light‐harvesting antennae by modifying pigment coupling

et al. 2020

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“…Out of up to 396 chemically identical but spectrally distinct linear tetrapyrroles covalently bound to a PB complex, 324 pigments are located in the peripheral rods. Each rod contains 2-3 phycocyanin hexamers that are characterized by room-temperature broad-band emission with the maximum near 650 nm [9][10][11][12][13]. In the core, 68 pigments bind to allophycocyanin with emission at~660 nm, while the remaining pigments are red-shifted further by~20 nm and form the so-called terminal emitters, which transfer excitation energy to the reaction centers [3,14].…”

Section: Introductionmentioning

confidence: 99%

Charge transfer states in phycobilisomes

Wahadoszamen¹,

Krüger²,

Ara³

et al. 2020

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…Numerous studies have demonstrated functional roles for the linker proteins that form the γ‐subunits in PE‐ and PC, most notably as regulators of different conformational states and fluorescence properties . Therefore, preserving γ‐subunit interactions in phycobiliprotein complexes, particularly their less stable association with PC, is likely crucial for maintaining their desired spectroscopic properties.…”

Section: Discussionmentioning

confidence: 99%

“…Numerous studies have demonstrated functional roles for the linker proteins that form the γ-subunits in PE-and PC, most notably as regulators of different conformational states and fluorescence properties. 12,26 Therefore, preserving γ-subunit interactions in phycobiliprotein complexes, particularly their less stable association with PC, is likely crucial for maintaining their desired spectroscopic properties. The possibilities offered by native MS to assess integrity and composition of phycobiliproteins as demonstrated here are evident, considering the widespread applications of phycobiliproteins as fluorescent probes in biotechnology, and particularly the continued efforts to find new natural sources.…”

Section: Discussionmentioning

confidence: 99%

A strategy for the identification of protein architectures directly from ion mobility mass spectrometry data reveals stabilizing subunit interactions in light harvesting complexes

et al. 2019

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Biotechnological applications of protein complexes require detailed information about their structure and composition, which can be challenging to obtain for proteins from natural sources. Prominent examples are the ring‐shaped phycoerythrin (PE) and phycocyanin (PC) complexes isolated from the light‐harvesting antennae of red algae and cyanobacteria. Despite their widespread use as fluorescent probes in biotechnology and medicine, the structures and interactions of their noncrystallizable central subunits are largely unknown. Here, we employ ion mobility mass spectrometry to reveal varying stabilities of the PC and PE complexes and identify their closest architectural homologues among all protein assemblies in the Protein Data Bank (PDB). Our results suggest that the central subunits of PC and PE complexes, although absent from the crystal structures, may be crucial for their stability, and thus of unexpected importance for their biotechnological applications.

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Phycocyanin: One Complex, Two States, Two Functions

Cited by 31 publications

References 39 publications

Marine cyanobacteria tune energy transfer efficiency in their light‐harvesting antennae by modifying pigment coupling

Marine cyanobacteria tune energy transfer efficiency in their light‐harvesting antennae by modifying pigment coupling

Charge transfer states in phycobilisomes

A strategy for the identification of protein architectures directly from ion mobility mass spectrometry data reveals stabilizing subunit interactions in light harvesting complexes

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