Integration of multiple chromophores with native photosynthetic antennas to enhance solar energy capture and delivery

Harris, Michelle A.; Parkes-Loach, Pamela S.; Springer, Joseph W.; Jiang, Jianbing; Martin, Elizabeth C.; Qian, Pu; Jiao, Jieying; Niedzwiedzki, Dariusz M.; Kirmaier, Christine; Olsen, John D.; Bocian, David F.; Holten, Dewey; Hunter, C. Neil; Lindsey, Jonathan S.; Loach, Paul A.

doi:10.1039/c3sc51518d

Cited by 38 publications

(69 citation statements)

References 54 publications

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“…4−6 The fastest energy transfer from the attached chromophores to dimeric and oligomeric BChl complexes (B820 and B875) were reported to occur in a time scale of 1− 10 ps. 5,6 The time resolution for both experiments are 100−150 fs (fwhm), which is short enough to observe subpicosecond . Geometrical description of LH2−A647 consisting of B800, B850, LH2 α-and β-polypeptides.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Extension of Light-Harvesting Ability of Photosynthetic Light-Harvesting Complex 2 (LH2) through Ultrafast Energy Transfer from Covalently Attached Artificial Chromophores

et al. 2015

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Introducing appropriate artificial components into natural biological systems could enrich the original functionality. To expand the available wavelength range of photosynthetic bacterial light-harvesting complex 2 (LH2 from Rhodopseudomonas acidophila 10050), artificial fluorescent dye (Alexa Fluor 647: A647) was covalently attached to N- and C-terminal Lys residues in LH2 α-polypeptides with a molar ratio of A647/LH2 ≃ 9/1. Fluorescence and transient absorption spectroscopies revealed that intracomplex energy transfer from A647 to intrinsic chromophores of LH2 (B850) occurs in a multiexponential manner, with time constants varying from 440 fs to 23 ps through direct and B800-mediated indirect pathways. Kinetic analyses suggested that B800 chromophores mediate faster energy transfer, and the mechanism was interpretable in terms of Förster theory. This study demonstrates that a simple attachment of external chromophores with a flexible linkage can enhance the light harvesting activity of LH2 without affecting inherent functions of energy transfer, and can achieve energy transfer in the subpicosecond range. Addition of external chromophores, thus, represents a useful methodology for construction of advanced hybrid light-harvesting systems that afford solar energy in the broad spectrum.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Extension of Light-Harvesting Ability of Photosynthetic Light-Harvesting Complex 2 (LH2) through Ultrafast Energy Transfer from Covalently Attached Artificial Chromophores

et al. 2015

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“…; see References ). Previous studies incorporated synthetic chromophores by covalent attachment to the β ‐peptide, which under proper conditions in the presence of the native α ‐peptide and BChl a self‐assemble to form the LH1‐type oligomer . A key feature of the proper conditions is the use of a detergent, which affords micelles or vesicles, given the membrane localization of the native photosynthetic antennas and hydrophobic nature of the α ‐ and β ‐peptides that comprise each subunit.…”

Section: Introductionmentioning

confidence: 99%

Enhanced Light‐Harvesting Capacity by Micellar Assembly of Free Accessory Chromophores and LH1‐like Antennas

Harris

Sahin

Jiang

et al. 2014

Photochem & Photobiology

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Biohybrid light-harvesting antennas are an emerging platform technology with versatile tailorability for solar-energy conversion. These systems combine the proven peptide scaffold unit utilized for light harvesting by purple photosynthetic bacteria with attached synthetic chromophores to extend solar coverage beyond that of the natural systems. Herein, synthetic unattached chromophores are employed that partition into the organized milieu (e.g. detergent micelles) that house the LH1-like biohybrid architectures. The synthetic chromophores include a hydrophobic boron-dipyrrin dye (A1) and an amphiphilic bacteriochlorin (A2), which transfer energy with reasonable efficiency to the bacteriochlorophyll acceptor array (B875) of the LH1-like cyclic oligomers. The energy-transfer efficiencies are markedly increased upon covalent attachment of a bacteriochlorin (B1 or B2) to the peptide scaffold, where the latter likely acts as an energy-transfer relay site for the (potentially diffusing) free chromophores. The efficiencies are consistent with a Förster (through-space) mechanism for energy transfer. The overall energy-transfer efficiency from the free chromophores via the relay to the target site can approach those obtained previously by relay-assisted energy transfer from chromophores attached at distant sites on the peptides. Thus, the use of free accessory chromophores affords a simple design to enhance the overall light-harvesting capacity of biohybrid LH1-like architectures.

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“…[2] Photosynthetic organisms use the electrons transported by photosystem I (PSI) to reduce NADP + to NADPH, but a number of biohybrid systems capable of harnessing these electrons to reduce protons to H 2 for solar fuels applications have been developed by linking PSI to synthetic catalysts. [3] These systems show that the unique photophysical properties imparted to natural chromophores embedded within the PSI reaction center protein scaffolds [4] can be exploited for non-natural chemical reactions.…”

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confidence: 99%

“…While a wide range of organic and organometallic cofactors have been incorporated into protein scaffolds to create artificial enzymes, [10] no systems in which a visible light photocatalyst that acts directly on an organic substrate is linked to a protein have been reported. We envisioned that such a system could be used to modulate the photophysical properties of visible light photocatalysts such as Acr + -Mes in analogy to natural systems [4] and ultimately impart selectivity to reactions catalyzed by these species. As a first step towards these goals, we describe the preparation and detailed characterization of an Acr + -Mes-based artificial enzyme that catalyzes sulfoxidation when irradiated with visible light in the presence of air.…”

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confidence: 99%

Preparation, Characterization, and Oxygenase Activity of a Photocatalytic Artificial Enzyme

Ellis‐Guardiola

Srivastava

et al. 2015

ChemBioChem

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A bicyclo[6,1,0]nonyne-substituted 9-mesityl-10-methyl-acridinium cofactor was prepared and covalently linked to a prolyl oligopeptidase scaffold containing a genetically encoded 4-azido-L-phenylalanine residue in its active site. The resulting artificial enzyme catalyzed sulfoxidation when irradiated with visible light in the presence of air. This reaction proceeds via initial electron abstraction from the sulfide within the enzyme active site, and the protein scaffold extended the fluorescence lifetime of the acridium cofactor. The mode of sulfide activation and placement of 5 in POP-ZA4-5 make this artificial enzyme a promising platform for developing selective photocatalytic transformations.

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Integration of multiple chromophores with native photosynthetic antennas to enhance solar energy capture and delivery

Cited by 38 publications

References 54 publications

Extension of Light-Harvesting Ability of Photosynthetic Light-Harvesting Complex 2 (LH2) through Ultrafast Energy Transfer from Covalently Attached Artificial Chromophores

Extension of Light-Harvesting Ability of Photosynthetic Light-Harvesting Complex 2 (LH2) through Ultrafast Energy Transfer from Covalently Attached Artificial Chromophores

Enhanced Light‐Harvesting Capacity by Micellar Assembly of Free Accessory Chromophores and LH1‐like Antennas

Preparation, Characterization, and Oxygenase Activity of a Photocatalytic Artificial Enzyme

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