Orientation and excitonic interactions of the Fenna-Matthews-Olson bacteriochlorophyll a protein in membranes of the green sulfur bacterium Chlorobium tepidum

Alexander N. Melkozernov, John M. Olson, Yi Fen Li, James Paul Allen, Robert E. Blankenship

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Linear and circular dichroism spectra of isolated bacteriochlorophyll a proteins (FMO proteins) and membrane vesicles containing FMO protein from the green sulfur bacterium Chlorobium tepidum were measured at room temperature and 77 K. The orientation of membranes and isolated FMO protein was obtained by gel squeezing. Linear dichroism (LD) data indicate that isolated FMO protein and membrane vesicles associated with the FMO protein are oriented in a similar way in a squeezed polyacrylamide gel. Both samples show a characteristic negative LD band around 814 nm with flanking positive bands at 802 and 824 nm ascribed to the Q(y) excitonic transitions of BChl a of the FMO protein. This confirms that the C3 symmetry axis of the trimer is perpendicular to the membrane plane, which is supported by the model of the disc-like structure of FMO protein trimers of Cb. tepidum [Li Yi-Fen, Zhou W, Blankenship RE, and Allen JP (1997) J Mol Biol 272:456-471]. The LD data are consistent with either BChl 3 or 6, but not 7 as the principal contributor to the low temperature band at 825 nm. The low temperature linear and circular dichroism spectra of FMO protein trimers from Chlorobium tepidum show significant differences from the low temperature LD and CD spectra of FMO protein trimers from Prosthecochloris aestuarii. The data are interpreted in terms of somewhat different pigment-protein and pigment-pigment interactions in the two complexes.

Original languageEnglish
Pages (from-to)315-328
Number of pages14
JournalPhotosynthesis Research
Volume56
Issue number3
DOIs
Publication statusPublished - 1998

Fingerprint

Chlorobium
Chlorobium tepidum
Chlorobi
Bacteriochlorophylls
Sulfur
membrane proteins
Bacteria
Membrane Proteins
Membranes
Proteins
proteins
Dichroism
Pigments
Temperature
circular dichroism spectroscopy
Circular Dichroism
pigments
R-SNARE Proteins
Prosthecochloris aestuarii
Chlorobiales

Keywords

  • Antenna
  • Bacteriochlorophyll a protein
  • Chlorobium tepidum
  • Circular dichroism
  • FMO protein
  • Linear dichroism

ASJC Scopus subject areas

  • Plant Science

Cite this

Orientation and excitonic interactions of the Fenna-Matthews-Olson bacteriochlorophyll a protein in membranes of the green sulfur bacterium Chlorobium tepidum. / Melkozernov, Alexander N.; Olson, John M.; Li, Yi Fen; Allen, James Paul; Blankenship, Robert E.

In: Photosynthesis Research, Vol. 56, No. 3, 1998, p. 315-328.

Research output: Contribution to journalArticle

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