ArticlePhotosynthesis research2013
Chemical oxidation of the FMO antenna protein from Chlorobaculum tepidum.
Article in Photosynthesis research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- Exciton Lifetime Distributions and Population Dynamics in the FMO Protein Complex fromACS omega · 2021Article
- The influence of quaternary structure on the stability of Fenna-Matthews-Olson (FMO) antenna complexes.Photosynthesis research · 2019Article
- Selective oxidation of B800 bacteriochlorophyll a in photosynthetic light-harvesting protein LH2.Scientific reports · 2019Article
- On uncorrelated inter-monomer Förster energy transfer in Fenna-Matthews-Olson complexes.Journal of the Royal Society, Interface · 2019Article
- Native FMO-reaction center supercomplex in green sulfur bacteria: an electron microscopy study.Photosynthesis research · 2016Article
- Hybrid QM/MM study of FMO complex with polarized protein-specific charge.Scientific reports · 2015Article
- On destabilization of the Fenna-Matthews-Olson complex of Chlorobaculum tepidum.Photosynthesis research · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Effect of chemical oxidation by ferricyanide on bacteriochlorophyll a (BChl a) in the Fenna-Matthews-Olson protein (FMO) was studied using absorbance and fluorescence spectroscopy at ambient and cryogenic temperatures. Partially selective oxidation of pigments bound to the antenna complex was achieved and the probable absorption wavelength corresponding to the recently discovered bacteriochlorophyll No. 8 of 806 nm was obtained by comparative analysis of the effect of chemical oxidation and the effect of different isolation procedures. Formation of a stable product identified as a chlorophyll a derivative occurred upon chemical oxidation. This new pigment remained bound within the pigment-protein complex, and exhibited an efficient energy transfer to BChl a. Furthermore, complex effects of the pigment oxidation upon the fluorescence yield of the FMO protein were observed. Utility of this approach based on chemical modifications for the investigation of the native regulatory mechanisms involved in the energy transfer in the FMO protein is discussed.
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