The microenvironment around the chromophores and its changes due to the association states in C-phycocyanin isolated from the cyanobacterium Mastigocladus laminosus

Mimuro, Mamoru; Rümbeli, Robert; Füglistaller, Paul; Zuber, Herbert

doi:10.1016/0005-2728(86)90081-2

Cited by 26 publications

(34 citation statements)

References 17 publications

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“…Therefore, we expect the α 84 + β 155 state to be the brightest of the three two-chromophore states, as observed here for S2. It is also known that both the absorption and emission spectra of β 155 are ∼20 nm blue-shifted compared with the α 84 -or β 84 -spectra (32,35), so the loss of the β 84 -pigment should result in a blue-shifted emission spectrum relative to the pristine state, as observed here for S2 (Fig. 4D).…”

Section: Applied Physical Sciencessupporting

confidence: 59%

“…We assign S2 to be the α 84 + β 155 state, shown here in green, primarily on the basis of its brightness and spectrum relative to the pristine state. It has been previously shown that β 155 acts as a sensitizer for β 84 (32,49); if β 84 is dark or photobleached, then β 155 will emit rather than transfer the bulk of its absorbed energy. Therefore, we expect the α 84 + β 155 state to be the brightest of the three two-chromophore states, as observed here for S2.…”

Section: Applied Physical Sciencesmentioning

confidence: 99%

“…1A). All three phycocyanobilins are chemically identical linear tetrapyrroles (31) with distinct photophysical properties directly conferred by their disparate conformations and chemical environments (32). The relative geometry of the three…”

mentioning

confidence: 99%

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Direct single-molecule measurements of phycocyanobilin photophysics in monomeric C-phycocyanin

Squires

Moerner

2017

Proc. Natl. Acad. Sci. U.S.A.

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Phycobilisomes are highly organized pigment-protein antenna complexes found in the photosynthetic apparatus of cyanobacteria and rhodophyta that harvest solar energy and transport it to the reaction center. A detailed bottom-up model of pigment organization and energy transfer in phycobilisomes is essential to understanding photosynthesis in these organisms and informing rational design of artificial light-harvesting systems. In particular, heterogeneous photophysical behaviors of these proteins, which cannot be predicted de novo, may play an essential role in rapid light adaptation and photoprotection. Furthermore, the delicate architecture of these pigment-protein scaffolds sensitizes them to external perturbations, for example, surface attachment, which can be avoided by study in free solution or in vivo. Here, we present single-molecule characterization of C-phycocyanin (C-PC), a threepigment biliprotein that self-assembles to form the midantenna rods of cyanobacterial phycobilisomes. Using the Anti-Brownian Electrokinetic (ABEL) trap to counteract Brownian motion of single particles in real time, we directly monitor the changing photophysical states of individual C-PC monomers from Spirulina platensis in free solution by simultaneous readout of their brightness, fluorescence anisotropy, fluorescence lifetime, and emission spectra. These include single-chromophore emission states for each of the three covalently bound phycocyanobilins, providing direct measurements of the spectra and photophysics of these chemically identical molecules in their native protein environment. We further show that a simple Förster resonant energy transfer (FRET) network model accurately predicts the observed photophysical states of C-PC and suggests highly variable quenching behavior of one of the chromophores, which should inform future studies of higherorder complexes.photosynthetic protein | C-phycocyanin | ABEL trap | single-molecule spectroscopy | photodynamics P hotosynthetic antenna structures based on pigment-protein complexes have garnered broad interest as model systems for solar energy harvesting that can directly inform development of alternative energy technologies (1). These systems transfer absorbed energy quickly and efficiently to reaction centers, and must rapidly adapt to changing irradiance to maintain photosynthetic efficiency while protecting against oxidative damage. These macroscopic behaviors of photosynthetic antenna systems are dictated by the nanoscale heterogeneous properties of the individual proteins from which they are assembled; therefore, constructing bottom-up models will be essential to fully understanding these systems. A variety of standard single-molecule techniques have been previously used to optically characterize individual antenna complexes and their substituent components, for example at low concentration (2-4) or immobilized on a surface (5-9) or in a polymer matrix (10). However, studying photosynthetic antenna proteins at the single-molecule level remains challenging (11) due to the...

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Section: Applied Physical Sciencessupporting

confidence: 59%

Section: Applied Physical Sciencesmentioning

confidence: 99%

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Direct single-molecule measurements of phycocyanobilin photophysics in monomeric C-phycocyanin

Squires

Moerner

2017

Proc. Natl. Acad. Sci. U.S.A.

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show abstract

“…The easiest and most explanatory spectroscopic test to determine the aggregation state of biliproteins is to record the excitation fluorescent steady‐state anisotropy spectrum (data not shown). Since energy transfer between chromophores modulates the fluorescent properties of these proteins, a dramatic increase in the anisotropy spectra has been observed when the aggregation state of the biliproteins changes from trimers to monomers,38, 39 due to the chromophores uncoupling, which altered the pathways for energy transfer between them. The spectra shapes and the quantitative values of the C‐PC are similar to those published earlier for trimeric C‐PC from S. platensis 38…”

Section: Resultsmentioning

confidence: 99%

Large‐scale isolation and purification of C‐phycocyanin from the cyanobacteria Anabaena marina using expanded bed adsorption chromatography

Ramos

Acién

Sevilla

et al. 2010

J of Chemical Tech & Biotech

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“…The easiest and most explanatory spectroscopic test to determine the aggregation state of biliproteins is to record the excitation fluorescent steady-state anisotropy spectrum (data not shown). Since energy transfer between chromophores modulates the fluorescent properties of these proteins, a dramatic increase in the anisotropy spectra has been observed when the aggregation state of the biliproteins changes from trimers to monomers [16,24,36], due to the chromophores uncoupling, which altered the pathways for energy transfer between them. The spectra shapes and the quantitative values of the C-PC are similar to those published earlier for trimeric C-PC from S. platensis [16,24].…”

Section: Purification and Identification Of C-pcmentioning

confidence: 99%

Development of a process for large-scale purification of C-phycocyanin from Synechocystis aquatilis using expanded bed adsorption chromatography

Ramos

Acién

Sevilla

et al. 2011

Journal of Chromatography B

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The microenvironment around the chromophores and its changes due to the association states in C-phycocyanin isolated from the cyanobacterium Mastigocladus laminosus

Cited by 26 publications

References 17 publications

Direct single-molecule measurements of phycocyanobilin photophysics in monomeric C-phycocyanin

Direct single-molecule measurements of phycocyanobilin photophysics in monomeric C-phycocyanin

Large‐scale isolation and purification of C‐phycocyanin from the cyanobacteria Anabaena marina using expanded bed adsorption chromatography

Development of a process for large-scale purification of C-phycocyanin from Synechocystis aquatilis using expanded bed adsorption chromatography

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