Reinterpretation of the electron density at the site of the eighth bacteriochlorophyll in the FMO protein from Pelodictyon phaeum Public Deposited

http://ir.library.oregonstate.edu/concern/defaults/sb397905g

This is the author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer and can be found at:  http://www.springer.com/life+sciences/plant+sciences/journal/11120.

Descriptions

Attribute NameValues
Creator
Abstract or Summary
  • The Fenna-Matthews-Olson antenna protein from the green bacterium Pelodictyon phaeum mediates the energy transfer from a peripheral antenna complex to the membrane-bound reaction center. The three-dimensional structure of this protein has been previously modeled using X-ray diffraction to a resolution limit of 2.0 Å, with R[subscript work] and R[subscript free] values of 16.6% and 19.9% respectively (Larson et al. (2011) Photosyn Res 107: 139–150). This model shows the protein as consisting of β-sheets surrounding several bacteriochlorophyll cofactors. While most of the model clearly matches the electron density maps, in this paper we re-examine the electron density for a specific feature, namely the eighth bacteriochlorophyll a cofactor. This electron density is now interpreted as arising primarily from the end of an otherwise disordered polyethylene glycol molecule. Additional electron density is present but the density is weak and cannot be unambiguously assigned. The new model has R[subscript work] and R[subscript free] values of 16.2% and 19.0%, respectively.
Resource Type
DOI
Date Available
Date Issued
Citation
  • Tronrud, D. E., & Allen, J. P. (2012, April). Reinterpretation of the electron density at the site of the eighth bacteriochlorophyll in the FMO protein from Pelodictyon phaeum. Photosynthesis Research, 112(1), 71-74. doi:10.1007/s11120-012-9735-8
Academic Affiliation
Series
Keyword
Rights Statement
Funding Statement (additional comments about funding)
Publisher
Peer Reviewed
Language
Replaces
Additional Information
  • description.provenance : Submitted by Deanne Bruner (deanne.bruner@oregonstate.edu) on 2013-01-16T21:34:57Z No. of bitstreams: 1 TronrudDaleBiochemistryBiophysicsReinterpretationElectronDensity.pdf: 177040 bytes, checksum: dcdbe27b634be9b935e58e44f85d566f (MD5)
  • description.provenance : Made available in DSpace on 2013-01-16T21:35:41Z (GMT). No. of bitstreams: 1 TronrudDaleBiochemistryBiophysicsReinterpretationElectronDensity.pdf: 177040 bytes, checksum: dcdbe27b634be9b935e58e44f85d566f (MD5) Previous issue date: 2012-04
  • description.provenance : Approved for entry into archive by Deanne Bruner(deanne.bruner@oregonstate.edu) on 2013-01-16T21:35:41Z (GMT) No. of bitstreams: 1 TronrudDaleBiochemistryBiophysicsReinterpretationElectronDensity.pdf: 177040 bytes, checksum: dcdbe27b634be9b935e58e44f85d566f (MD5)

Relationships

In Administrative Set:
Last modified: 07/11/2017

Downloadable Content

Download PDF
Citations:

EndNote | Zotero | Mendeley

Items