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Single-Molecule Fluorescence Spectroscopy of Photosynthetic Systems
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Photosynthesis begins when a network of pigment-protein complexes captures solar energy and transports it to the reaction center, where charge separation occurs. When necessary (under low light conditions), photosynthetic organisms perform this energy transport and charge separation with near unity quantum efficiency. Remarkably, this high efficiency is maintained under physiological conditions, which include thermal fluctuations of the pigment-protein complexes and changing local environments. These conditions introduce multiple types of heterogeneity in the pigment-protein complexes, including structural heterogeneity, energetic heterogeneity, and functional heterogeneity. Understanding how photosynthetic light-harvesting functions in the face of these fluctuations requires understanding this heterogeneity, which, in turn, requires characterization of individual pigment-protein complexes. Single-molecule spectroscopy has the power to probe individual complexes. In this review, we present an overview of the common techniques for single-molecule fluorescence spectroscopy applied to photosynthetic systems and describe selected experiments on these systems. We discuss how these experiments provide a new understanding of the impact of heterogeneity on light harvesting and thus how these systems are optimized to capture sunlight under physiological conditions.
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“Recently, developments in experimental techniques such as ultrafast spectroscopy [6], single molecule spectroscopy [7 -11], timeresolved microscopy [12 -14] and single particle imaging [15 -18] have enabled us to study biological dynamics on increasingly small length and time scales, revealing a variety of processes necessary for the function of the living system that depend on a delicate interpl”
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Metadata
- Authors
- Kondo, T., Chen, W. J., & Schlau-Cohen, G. S.
- Affiliations
- Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge Massachusetts 02139, United States
- Massachusetts Institute of Technology (US)
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2017-01-10
- Volume
- 117
- Issue
- 2
- Pages
- 860-898
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2568620643
- Cited by
- 120
- References
- 320
- Citations by year
- 2026: 6 · 2025: 13 · 2024: 16 · 2023: 10 · 2022: 16 · 2021: 11 · 2020: 13 · 2019: 10 · 2018: 16 · 2017: 9
- FWCI
- 0.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.osti.gov
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Richard and Susan Smith Family Foundation (Excellence in Biomedical Research Award)
- Basic Energy Sciences (Center for Excitonics/DE-SC0001088)
- Topics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Keywords
- photosynthesis, light-harvesting complexes, single-molecule fluorescence spectroscopy, pigment-protein complexes, structural heterogeneity, energetic heterogeneity, functional heterogeneity, thermal fluctuations, energy transport, charge separation, reaction center, quantum efficiency, low-light adaptation
- MeSH terms
- Photosynthesis, Pigments, Biological, Proteins, Spectrometry, Fluorescence
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