DOI: 10.1073/pnas.0901691106. Membrane orientation of the FMO antenna protein from <i>Chlorobaculum tepidum</i> as determined by mass spectrometry-based footprinting

Membrane orientation of the FMO antenna protein from Chlorobaculum tepidum as determined by mass spectrometry-based footprinting

10.1073/pnas.0901691106

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

The high excitation energy-transfer efficiency demanded in photosynthetic organisms relies on the optimal pigment-protein binding orientation in the individual protein complexes and also on the overall architecture of the photosystem. In green sulfur bacteria, the membrane-attached Fenna-Matthews-Olson (FMO) antenna protein functions as a “wire” to connect the large peripheral chlorosome antenna complex with the reaction center (RC), which is embedded in the cytoplasmic membrane (CM). Energy collected by the chlorosome is funneled through the FMO to the RC. Although there has been considerable effort to understand the relationships between structure and function of the individual isolated complexes, the specific architecture for in vivo interactions of the FMO protein, the CM, and the chlorosome, ensuring highly efficient energy transfer, is still not established experimentally. Here, we describe a mass spectrometry-based method that probes solvent-exposed surfaces of the FMO by labeling solvent-exposed aspartic and glutamic acid residues. The locations and extents of labeling of FMO on the native membrane in comparison with it alone and on a chlorosome-depleted membrane reveal the orientation. The large differences in the modification of certain peptides show that the Bchl a #3 side of the FMO trimer interacts with the CM, which is consistent with recent theoretical predictions. Moreover, the results also provide direct experimental evidence to confirm the overall architecture of the photosystem from Chlorobaculum tepidum ( C. tepidum ) and give information on the packing of the FMO protein in its native environment.

Bibliography

Wen, J., Zhang, H., Gross, M. L., & Blankenship, R. E. (2009). Membrane orientation of the FMO antenna protein from Chlorobaculum tepidum as determined by mass spectrometry-based footprinting. Proceedings of the National Academy of Sciences, 106(15), 6134â6139.

Authors 4

Jianzhong Wen (first)
Hao Zhang (additional)
Michael L. Gross (additional)
Robert E. Blankenship (additional)

References 39 Referenced 184

10.1002/9780470758472
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DE Tronrud JZ Wen L Gay RE Blankenship The structural difference in absorbance spectra for the FMO protein from green sulfur bacteria (submitted). 2009). (10.1007/s11120-009-9430-6)
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M Mohseni, P Rebentrost, S Lloyd, A Aspuru-Guzik, Environment-assisted quantum walks in energy transfer of photosynthetic complexes. Quantum Physics, arXiv:0805.2741v1. (2008). / Quantum Physics / Environment-assisted quantum walks in energy transfer of photosynthetic complexes by Mohseni M (2008)
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Dates

Type	When
Created	16 years, 5 months ago (April 1, 2009, 9:10 p.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 6:01 p.m.)
Indexed	6 days ago (Aug. 29, 2025, 6:11 a.m.)
Issued	16 years, 4 months ago (April 14, 2009)
Published	16 years, 4 months ago (April 14, 2009)
Published Online	16 years, 4 months ago (April 14, 2009)
Published Print	16 years, 4 months ago (April 14, 2009)

Funders 0

None

BibTeX

@article{Wen_2009, title={Membrane orientation of the FMO antenna protein from Chlorobaculum tepidum as determined by mass spectrometry-based footprinting}, volume={106}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0901691106}, DOI={10.1073/pnas.0901691106}, number={15}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Wen, Jianzhong and Zhang, Hao and Gross, Michael L. and Blankenship, Robert E.}, year={2009}, month=apr, pages={6134–6139} }

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