Photosynthetic Pigment-protein Complexes Research Articles

Hidden vibronic and excitonic structure and vibronic coherence transfer in the bacterial reaction center.

We report two-dimensional electronic spectroscopy (2DES) experiments on the bacterial reaction center (BRC) from purple bacteria, revealing hidden vibronic and excitonic structure. Through analysis of the coherent dynamics of the BRC, we identify multiple quasi-resonances between pigment vibrations and excitonic energy gaps, and vibronic coherence transfer processes that are typically neglected in standard models of photosynthetic energy transfer and charge separation. We support our assignment with control experiments on bacteriochlorophyll and simulations of the coherent dynamics using a reduced excitonic model of the BRC. We find that specific vibronic coherence processes can readily reveal weak exciton transitions. While the functional relevance of such processes is unclear, they provide a spectroscopic tool that uses vibrations as a window for observing excited state structure and dynamics elsewhere in the BRC via vibronic coupling. Vibronic coherence transfer reveals the upper exciton of the “special pair” that was weakly visible in previous 2DES experiments.

Towards a quantitative description of excitonic couplings in photosynthetic pigment-protein complexes: quantum chemistry driven multiscale approaches.

A structure-based quantitative calculation of excitonic couplings between photosynthetic pigments has to describe the dynamical polarization of the protein/solvent environment of the pigments, giving rise to reaction field and screening effects. Here, this challenging problem is approached by combining the fragment molecular orbital (FMO) method with the polarizable continuum model (PCM). The method is applied to compute excitonic couplings between chlorophyll a (Chl a) pigments of the water-soluble chlorophyll-binding protein (WSCP). By calibrating the vacuum dipole strength of the 0–0 transition of the Chl a chromophores according to experimental data, an excellent agreement between calculated and experimental linear absorption and circular dichroism spectra of WSCP is obtained. The effect of the mutual polarization of the pigment ground states is calculated to be very small. The simple Poisson-Transition-charge-from-Electrostatic-potential (Poisson-TrEsp) method is found to accurately describe the screening part of the excitonic coupling, obtained with FMO/PCM. Taking into account that the reaction field effects of the latter method can be described by a scalar constant leads to an improvement of Poisson-TrEsp that is expected to provide the basis for simple and realistic calculations of optical spectra and energy transfer in photosynthetic light-harvesting complexes. In addition, we present an expression for the estimation of Huang–Rhys factors of high-frequency pigment vibrations from experimental fluorescence line-narrowing spectra that takes into account the redistribution of oscillator strength by the interpigment excitonic coupling. Application to WSCP results in corrected Huang–Rhys factors that are less than one third of the original values obtained by the standard electronic two-state analysis that neglects the above redistribution. These factors are important for the estimation of the dipole strength of the 0–0 transition of the chromophores and for the development of calculation schemes for the spectral density of the exciton-vibrational coupling.

Ultrafast laser spectroscopic studies on carotenoids in solution and on those bound to photosynthetic pigment-protein complexes.

Carotenoid excited singlet states, in particular, are typically very short lived. Therefore, time-resolved absorption spectroscopy in the time regime from femtoseconds to sub-milliseconds are required to unravel and understand the complicated relaxation and excitation energy-transfer pathways of carotenoids in solution and in photosynthetic pigment-protein complexes. The focus of this chapter is to explain how to use ultrafast time-resolved absorption spectroscopy in carotenoid research. The importance of a systematic approach to understanding the various carotenoid excited states by using a series of carotenoids with different conjugation lengths and the isomers of carotenoids is also emphasized.

Redox conditions correlated with vibronic coupling modulate quantum beats in photosynthetic pigment–protein complexes

Quantum coherences, observed as time-dependent beats in ultrafast spectroscopic experiments, arise when light-matter interactions prepare systems in superpositions of states with differing energy and fixed phase across the ensemble. Such coherences have been observed in photosynthetic systems following ultrafast laser excitation, but what these coherences imply about the underlying energy transfer dynamics remains subject to debate. Recent work showed that redox conditions tune vibronic coupling in the Fenna-Matthews-Olson (FMO) pigment-protein complex in green sulfur bacteria, raising the question of whether redox conditions may also affect the long-lived (>100 fs) quantum coherences observed in this complex. In this work, we perform ultrafast two-dimensional electronic spectroscopy measurements on the FMO complex under both oxidizing and reducing conditions. We observe that many excited-state coherences are exclusively present in reducing conditions and are absent or attenuated in oxidizing conditions. Reducing conditions mimic the natural conditions of the complex more closely. Further, the presence of these coherences correlates with the vibronic coupling that produces faster, more efficient energy transfer through the complex under reducing conditions. The growth of coherences across the waiting time and the number of beating frequencies across hundreds of wavenumbers in the power spectra suggest that the beats are excited-state coherences with a mostly vibrational character whose phase relationship is maintained through the energy transfer process. Our results suggest that excitonic energy transfer proceeds through a coherent mechanism in this complex and that the coherences may provide a tool to disentangle coherent relaxation from energy transfer driven by stochastic environmental fluctuations.

Photosynthetic pigment-protein complexes optical response modeling optimized by Differential evolution: algorithm convergence study

Photosynthetic pigment-protein complexes are the essential parts of thylakoid membranes of higher plants and cyanobacteria. Besides many organic and inorganic molecules they contain pigments like chlorophyll, bacteriochlorophyll, and carotenoids, which absorb the incident light and transform it into the energy of the excited electronic states. The semiclassical theories such as molecular exciton theory and the multimode Brownian oscillator model allows us to simulate the linear and nonlinear optical response of any pigment-protein complex, however, the main disadvantage of those approaches is a significant amount of effective parameters needed to be found in order to reproduce the experimental data. To overcome these difficulties we used the Differential evolution method (DE) that belongs to the family of evolutionary optimization algorithms. Based on our preliminary studies of the linear optical properties of monomeric photosynthetic pigments using DE, we proceed to more complex systems like the reaction center of photosystem II isolated from higher plants (PSIIRC). PSIIRC contains only eight chlorophyll pigments, and therefore it is potentially a very promising subject to test DE as a powerful optimization procedure for simulation of the optical response of a system of interacting pigments. Using the theoretically simulated linear spectra of PSIIRC (absorption, circular dichroism, linear dichroism, and fluorescence), we investigated the dependence of the algorithm convergence on DE settings: strategies, crossover, weighting factor; eventually finding the optimal mode of operation of the optimization procedure.

Accurate prediction of mutation-induced frequency shifts in chlorophyll proteins with a simple electrostatic model.

Photosynthetic pigment-protein complexes control local chlorophyll (Chl) transition frequencies through a variety of electrostatic and steric forces. Site-directed mutations can modify this local spectroscopic tuning, providing critical insight into native photosynthetic functions and offering the tantalizing prospect of creating rationally designed Chl proteins with customized optical properties. Unfortunately, at present, no proven methods exist for reliably predicting mutation-induced frequency shifts in advance, limiting the method's utility for quantitative applications. Here, we address this challenge by constructing a series of pointmutants in the water-soluble chlorophyll protein of Lepidium virginicum and using them to test the reliability of a simple computational protocol for mutation-induced site energy shifts. The protocol uses molecular dynamics to prepare mutant protein structures and the charge density coupling model of Adolphs et al. [Photosynth. Res. 95, 197-209 (2008)] for site energy prediction; a graphical interface that implements the protocol automatically is published online at http://nanohub.org/tools/pigmenthunter. With the exception of a single outlier (presumably due to unexpected structural changes), we find that the calculated frequency shifts match the experiment remarkably well, with an average error of 1.6nm over a 9nm spread in wavelengths. We anticipate that the accuracy of the method can be improved in the future with more advanced sampling of mutant protein structures.

Light Induced Changes in Pigment and Lipid Profiles of Bryopsidales Algae

Bryopsidales (Chlorophyta) are cultured and consumed in several regions of the planet and are known for their high nutritional value and bioprospection potential, due to a high content of relevant polar lipids and polysaccharides. Among other characteristic features, these marine algae are known for possessing unique photosynthetic pigment-protein complexes and for the absence (in nearly all species investigated) of a functional xanthophyll cycle, a ubiquitous photoprotection mechanism present in most algae and plants. With the aim of characterizing the photophysiology of this atypical group of algae, we investigated the changes in pigment content and polar lipidome of two Bryopsidales species (Codium tomentosumandBryopsis plumosa) exposed for 7 days to low or high irradiance (20 vs. 1,000 μmol photons m–2s–1). Our results show that high light has a strong effect on the pigment composition, triggering the time-dependent accumulation of all-trans-neoxanthin (t-Neo) and violaxanthin (Viola). High light-acclimated macroalgae also displayed a shift in the characteristic polar lipidome, including a trend of accumulation of lyso-glycolipids, and highly unsaturated phospholipids and betaine lipids. We hypothesize that the observed shifts on the lipid composition could promote the interaction betweent-Neo and Viola with the siphonaxanthin–chlorophyll–protein complexes (SCP) of photosystem II (PSII) within the thylakoid membranes of the chloroplasts. Light induced changes in pigment and lipid composition could contribute to the fitness of Bryopsidales algae by reducing damages to the photosynthetic apparatus under increased irradiance.

Insights into Solution Structures of Photosynthetic Protein Complexes from Small-Angle Scattering Methods

High-resolution structures of photosynthetic pigment–protein complexes are often determined using crystallography or cryo-electron microscopy (cryo-EM), which are restricted to the use of protein crystals or to low temperatures, respectively. However, functional studies and biotechnological applications of photosystems necessitate the use of proteins isolated in aqueous solution, so that the relevance of high-resolution structures has to be independently verified. In this regard, small-angle neutron and X-ray scattering (SANS and SAXS, respectively) can serve as the missing link because of their capability to provide structural information for proteins in aqueous solution at physiological temperatures. In the present review, we discuss the principles and prototypical applications of SANS and SAXS using the photosynthetic pigment–protein complexes phycocyanin (PC) and Photosystem I (PSI) as model systems for a water-soluble and for a membrane protein, respectively. For example, the solution structure of PSI was studied using SAXS and SANS with contrast matching. A Guinier analysis reveals that PSI in solution is virtually free of aggregation and characterized by a radius of gyration of about 75 Å. The latter value is about 10% larger than expected from the crystal structure. This is corroborated by an ab initio structure reconstitution, which also shows a slight expansion of Photosystem I in buffer solution at room temperature. In part, this may be due to conformational states accessible by thermally activated protein dynamics in solution at physiological temperatures. The size of the detergent belt is derived by comparison with SANS measurements without detergent match, revealing a monolayer of detergent molecules under proper solubilization conditions.

Two-photon absorption and excitation spectroscopy of carotenoids, chlorophylls and pigment-protein complexes.

In addition to (bacterio)chlorophylls, (B)Chls, photosynthetic pigment-protein complexes bind carotenoids (Cars) that fulfil various important functions which are not fully understood, yet. However, certain excited states of Cars are optically one-photon forbidden ("dark") and can potentially undergo excitation energy transfer (EET) to (B)Chls following two-photon absorption (TPA). The amount of EET is reflected by the differences in TPA and two-photon excitation (TPE) spectra of a complex (multi-pigment) system. Since it is technically and analytically demanding to resolve optically forbidden states, different studies reported varying contributions of Cars and Chls to TPE/TPA spectra. In a study using well-defined 1 : 1 Car-tetrapyrrole dyads TPE contributions of tetrapyrrole molecules, including Chls, and Cars were measured. In these experiments, TPE of Cars dominated over Chl a TPE in a broad wavelength range. Another study suggested only minor contributions of Cars to TPE spectra of pigment-protein complexes such as the plant main light-harvesting complex (LHCII), in particular for wavelengths longer than ∼600/1200 nm. By joining forces and a combined analysis of all available data by both teams, we try to resolve this apparent contradiction. Here, we demonstrate that reconstruction of a wide spectral range of TPE for LHCII and photosystem I (PSI) requires both, significant Car and Chl contributions. Direct comparison of TPE spectra obtained in both studies demonstrates a good agreement of the primary data. We conclude that in TPE spectra of LHCII and PSI, the contribution of Chls is dominating above 600/1200 nm, whereas the contributions of forbidden Car states increase particularly at wavelengths shorter than 600/1200 nm. Estimates of Car contributions to TPA as well as TPE spectra are given for various wavelengths.

Production of Carotenoids from Cultivated Seaweed.

Cladosiphon (C.) okamuranus, a brown alga endemic to the Nansei Islands, Japan, has been conventionally ingested as food. Nowadays, it is a major aquatic product of the Okinawa Prefecture with an annual production of around 20,000 tons. The life cycle of C. okamuranus comprises the macroscopic sporophyte (algal body) generation and the microscopic gametophyte generation. The germlings in the latter generation can proliferate when floating in seawater. This floating form has been exploited in techniques involved in the commercial production of C. okamuranus seedlings.Brown algae contain fucoxanthin, a carbonyl carotenoid known to have anticancer, anti-obesity, and antidiabetic effect in addition to the anti-oxidation effect. We found that the fucoxanthin content of cultivated floating form of C. okamuranus discoid germlings becomes up to 50 times that of the mature alga. Since the discoid germlings repeatedly grow like microorganisms, although they are large algae, they are utilized to produce fucoxanthin. We optimize the culture conditions by changing the temperature, light intensity, photoperiod, light wavelength, and nutrient salt conditions for optimal fucoxanthin productivity. The cultivation has been successful to industrial plant scale, culminating in the use of 1 ton of cultivating medium.In brown algal cells, fucoxanthin is primarily found bound to the photosynthetic pigment-protein complexes known as fucoxanthin-chlorophyll protein (FCP). Consequently cultivated floating form of C. okamuranus also shows high content of FCP. Isolation and characterization of pigments bound to the FCP were determined precisely, and ultrafast spectroscopies were applied to elucidate the photosynthetic function of fucoxanthin bound to the pigment-protein complexes. This cultivation method has also been applied to the other edible brown algae. We found that the optimal cultivation conditions as well as the yields of fucoxanthin and FCP highly depend on the species.The floating form cultivation was also applied to a large-sized edible green alga, Codium intricatum, which is uniquely producing a carbonyl carotenoid, siphonaxanthin. This has several anti-disease effects and is also a primal photosynthetic pigment which is found bound to photosynthetic antenna complex usually called siphonaxanthin-chlorophyll protein (SCP). We are working on the improvement of productivity, scale-up of production, and development of cultivation technology of new macro algae.

Photovoltage generation by photosystem II core complexes immobilized onto a Millipore filter on an indium tin oxide electrode.

The light-induced functioning of photosynthetic pigment-protein complex of photosystem II (PSII) is linked to the vectorial translocation of charges across the membrane, which results in the formation of voltage. Direct measurement of the light-induced voltage (∆V) generated by spinach oxygen-evolving PSII core complexes adsorbed onto a Millipore membrane filter (MF) on an indium tin oxide (ITO) electrode under continuous illumination has been performed. PSII was shown to participate in electron transfer from water to the ITO electrode, resulting in ∆V generation. No photovoltage was detected in PSII deprived of the water-oxidizing complex. The maximal and stable photoelectric signal was observed in the presence of disaccharide trehalose and 2,6-dichloro-1,4-benzoquinone, acting as a redox mediator between the primary quinone acceptor QA of PSII and electrode surface. Long time preservation of the steady-state photoactivity at room temperature in a simple in design ITO|PSII-MF|ITO system may be related to the retention of water molecules attached to the PSII surface in the presence of trehalose.

Delocalization Effects in Chlorophyll Fluorescence: Nonperturbative Line Shape Analysis of a Vibronically Coupled Dimer.

Non-adiabatic vibrational/electronic (vibronic) interactions in photosynthetic pigment/protein complexes (PPCs) have recently attracted considerable interest as a potential source for long-lived dynamic coherence and optimized light harvesting. The analysis of such effects is limited, however, by the complexity of the vibrational spectrum of biological pigments such as chlorophyll (Chl) molecules, which often makes numerical calculations prohibitively expensive and complicates the interpretation of experimental spectroscopic data. This work contributes to both challenges by using numerically exact computational methods to systematically examine vibronic mixing effects in the low-temperature fluorescence spectra of a Chl dimer possessing a full complement of local vibrations, using parameters extracted from experimental data. The results highlight the varying roles local vibrations can play in energy-transfer dynamics, both enhancing delocalization through vibronic resonance and, conversely, inducing dynamic localization by acting as a "self-bath" for local electronic transitions. In the specific context of line-narrowed fluorescence, the results indicate that, while low-frequency features are strongly suppressed by delocalization, high-frequency modes are likely to be dynamically localized in the parameter regime relevant to most photosynthetic complexes.

Quantum simulation dynamics and circuit synthesis of FMO complex on an NMR quantum computer

Recently, the dynamics simulation of light-harvesting complexes as an open quantum system, in the weak and strong coupling regimes, has received much attention. In this paper, we investigate a digital quantum simulation approach of the Fenna–Matthews–Olson (FMO) photosynthetic pigment-protein complex surrounded with a Markovian bath, i.e. memoryless, based on a nuclear magnetic resonance (NMR) quantum computer. For this purpose, we apply the decoupling (recoupling) method, which is turn off (on) the couplings, and also Solovay–Kitaev techniques to decompose Hamiltonian and Lindbladians into efficient elementary gates on an NMR simulator. Finally, we design the quantum circuits for the unitary and nonunitary part due to the system-environment interactions of the open system dynamics.

The chirality origin of retinal-carotenoid complex in gloeobacter rhodopsin: a temperature-dependent excitonic coupling

Retinal proteins play significant roles in light-induced protons/ions transport across the cell membrane. A recent studied retinal protein, gloeobacter rhodopsin (gR), functions as a proton pump, and binds the carotenoid salinixanthin (sal) in addition to the retinal chromophore. We have studied the interactions between the two chromophores as reflected in the circular dichroism (CD) spectrum of gR complex. gR exhibits a weak CD spectrum but following binding of sal, it exhibits a significant enhancement of the CD bands. To examine the CD origin, we have substituted the retinal chromophore of gR by synthetic retinal analogues, and have concluded that the CD bands originated from excitonic interaction between sal and the retinal chromophore as well as the sal chirality induced by binding to the protein. Temperature increase significantly affected the CD spectra, due to vanishing of excitonic coupling. A similar phenomenon of excitonic interaction lose between chromophores was recently reported for a photosynthetic pigment-protein complex (Nature Commmun, 9, 2018, 99). We propose that the excitonic interaction in gR is weaker due to protein conformational alterations. The excitonic interaction is further diminished following reduction of the retinal protonated Schiff base double bond. Furthermore, the intact structure of the retinal ring is necessary for obtaining the excitonic interaction.

Solid state organic photovoltaic devices using spirulina sp thylakoid membrane films as active material

Efficient light-to-energy conversion in Photosynthetis proceeds with quantum efficiency near unity. However, solar cell devices which incorporates chlorophyll such as DSSC generally requires elaborate fabrication process and complex device structure with liquid electrolyte. In this work, a solid state organic solar cell device is presented. The device employs simple structure of ITO/Thylakoid membrane/Al layer in a solid state structure without require liquid electrolyte. As the active materials, Thylakoid membrane layer contains the whole photosynthetic pigment-protein complexes including Photosystem I and Photosystem II. Preliminary characterization of the solid state organic photovoltaic devices exhibits modest ISC of 0.44 μA, VOC of 0.17 V, and Fill Factor of 0.250 when illuminated under the 1 mW/cm2 incandescent radiation power. Plot of (αhv)2 against the (hv) for tyakoid membrane active materials reveals major optical band-gap values of 4.0–4.1 eV which corresponds to the absorbtion from the PS I and PS II light harvesting complexes. This encouraging result implies that incorporating the whole photosynthetic pigment-protein complex can enhance the performance of organic solar cell significantly.

Silver Island Film for Enhancing Light Harvesting in Natural Photosynthetic Proteins.

The effects of combining naturally evolved photosynthetic pigment–protein complexes with inorganic functional materials, especially plasmonically active metallic nanostructures, have been a widely studied topic in the last few decades. Besides other applications, it seems to be reasonable using such hybrid systems for designing future biomimetic solar cells. In this paper, we describe selected results that point out to various aspects of the interactions between photosynthetic complexes and plasmonic excitations in Silver Island Films (SIFs). In addition to simple light-harvesting complexes, like peridinin-chlorophyll-protein (PCP) or the Fenna–Matthews–Olson (FMO) complex, we also discuss the properties of large, photosynthetic reaction centers (RCs) and Photosystem I (PSI)—both prokaryotic PSI core complexes and eukaryotic PSI supercomplexes with attached antenna clusters (PSI-LHCI)—deposited on SIF substrates.

Vibronic mixing enables ultrafast energy flow in light-harvesting complex II

Since the discovery of quantum beats in the two-dimensional electronic spectra of photosynthetic pigment-protein complexes over a decade ago, the origin and mechanistic function of these beats in photosynthetic light-harvesting has been extensively debated. The current consensus is that these long-lived oscillatory features likely result from electronic-vibrational mixing, however, it remains uncertain if such mixing significantly influences energy transport. Here, we examine the interplay between the electronic and nuclear degrees of freedom (DoF) during the excitation energy transfer (EET) dynamics of light-harvesting complex II (LHCII) with two-dimensional electronic-vibrational spectroscopy. Particularly, we show the involvement of the nuclear DoF during EET through the participation of higher-lying vibronic chlorophyll states and assign observed oscillatory features to specific EET pathways, demonstrating a significant step in mapping evolution from energy to physical space. These frequencies correspond to known vibrational modes of chlorophyll, suggesting that electronic-vibrational mixing facilitates rapid EET over moderately size energy gaps.

A photosynthetic antenna complex foregoes unity carotenoid-to-bacteriochlorophyll energy transfer efficiency to ensure photoprotection

Carotenoids play a number of important roles in photosynthesis, primarily providing light-harvesting and photoprotective energy dissipation functions within pigment-protein complexes. The carbon-carbon double bond (C=C) conjugation length of carotenoids (N), generally between 9 and 15, determines the carotenoid-to-(bacterio)chlorophyll [(B)Chl] energy transfer efficiency. Here we purified and spectroscopically characterized light-harvesting complex 2 (LH2) from Rhodobacter sphaeroides containing the N = 7 carotenoid zeta (ζ)-carotene, not previously incorporated within a natural antenna complex. Transient absorption and time-resolved fluorescence show that, relative to the lifetime of the S1 state of ζ-carotene in solvent, the lifetime decreases ∼250-fold when ζ-carotene is incorporated within LH2, due to transfer of excitation energy to the B800 and B850 BChls a These measurements show that energy transfer proceeds with an efficiency of ∼100%, primarily via the S1 → Qx route because the S1 → S0 fluorescence emission of ζ-carotene overlaps almost perfectly with the Qx absorption band of the BChls. However, transient absorption measurements performed on microsecond timescales reveal that, unlike the native N ≥ 9 carotenoids normally utilized in light-harvesting complexes, ζ-carotene does not quench excited triplet states of BChl a, likely due to elevation of the ζ-carotene triplet energy state above that of BChl a These findings provide insights into the coevolution of photosynthetic pigments and pigment-protein complexes. We propose that the N ≥ 9 carotenoids found in light-harvesting antenna complexes represent a vital compromise that retains an acceptable level of energy transfer from carotenoids to (B)Chls while allowing acquisition of a new, essential function, namely, photoprotective quenching of harmful (B)Chl triplets.

Predictive First-Principles Modeling of a Photosynthetic Antenna Protein: The Fenna-Matthews-Olson Complex.

High efficiency of light harvesting in photosynthetic pigment-protein complexes is governed by evolutionary-perfected protein-assisted tuning of individual pigment properties and interpigment interactions. Due to the large number of spectrally overlapping pigments in a typical photosynthetic complex, experimental methods often fail to unambiguously identify individual chromophore properties. Here, we report a first-principles-based modeling protocol capable of predicting properties of pigments in protein environment to a high precision. The technique was applied to successfully uncover electronic properties of the Fenna-Matthews-Olson (FMO) pigment-protein complex. Each of the three subunits of the FMO complex contains eight strongly coupled bacteriochlorophyll a (BChl a) pigments. The excitonic structure of FMO can be described by an electronic Hamiltonian containing excitation (site) energies of BChl a pigments and electronic couplings between them. Several such Hamiltonians have been developed in the past based on the information from various spectroscopic measurements of FMO; however, fine details of the excitonic structure and energy transfer in FMO, especially assignments of short-lived high-energy sites, remain elusive. Utilizing polarizable embedding quantum mechanics/molecular mechanics with the effective fragment potentials, we computed the electronic Hamiltonian of FMO that is in general agreement with previously reported empirical Hamiltonians and quantitatively reproduces experimental absorption and circular dichroism spectra of the FMO protein. The developed computational protocol is sufficiently simple and can be utilized for predictive modeling of other wild-type and mutated photosynthetic pigment-protein complexes.

DNA scaffold supports long-lived vibronic coherence in an indodicarbocyanine (Cy5) dimer.

Vibronic coupling between pigment molecules is believed to prolong coherences in photosynthetic pigment–protein complexes. Reproducing long-lived coherences using vibronically coupled chromophores in synthetic DNA constructs presents a biomimetic route to efficient artificial light harvesting. Here, we present two-dimensional (2D) electronic spectra of one monomeric Cy5 construct and two dimeric Cy5 constructs (0 bp and 1 bp between dyes) on a DNA scaffold and perform beating frequency analysis to interpret observed coherences. Power spectra of quantum beating signals of the dimers reveal high frequency oscillations that correspond to coherences between vibronic exciton states. Beating frequency maps confirm that these oscillations, 1270 cm−1 and 1545 cm−1 for the 0-bp dimer and 1100 cm−1 for the 1-bp dimer, are coherences between vibronic exciton states and that these coherences persist for ∼300 fs. Our observations are well described by a vibronic exciton model, which predicts the excitonic coupling strength in the dimers and the resulting molecular exciton states. The energy spacing between those states closely corresponds to the observed beat frequencies. MD simulations indicate that the dyes in our constructs lie largely internal to the DNA base stacking region, similar to the native design of biological light harvesting complexes. Observed coherences persist on the timescale of photosynthetic energy transfer yielding further parallels to observed biological coherences, establishing DNA as an attractive scaffold for synthetic light harvesting applications.