Structure In 1962, John Olson isolated a water-soluble bacteriochlorophyll (BChl a) protein (150 kDa) from green sulfur bacteria
(Olson and Romano 1962). This specific protein is part of the light-harvesting system in green sulfur bacteria where it acts as a subantenna to collect sunlight and transfer excitation energy from the light-harvesting antennas to the reaction center. Absorption 3-MA mouse spectroscopy on extracts of strains of Chlorobium showed that the newly discovered protein contained only BChl a chromophores, non-covalently bound to a protein envelope (Fig. 1). In 1975, Roger Fenna and Brian Matthews resolved the X-ray structure of the FMO protein from Prosthecochloris aestuarii at 2.8 Å resolution and found that the complex consists of three identical subunits related by C 3 symmetry, each containing seven BChl a pigments (Fenna and Matthews 1975). It showed a protein shell in which the BChl a molecules were enclosed. The major part of the outside of the protein shell exposed to the solvent is composed of 15 strands of β-sheet. The side of the shell that is in contact with one of the other subunits in the trimer consists of four short
strands of α-helix alternated by regions of the protein without a clear structure. The average distance between BChl a molecules within one subunit of the trimer is 12 Å while the nearest molecule in the neighboring subunit is found at a distance
of 24 Å. Analysis of the Linsitinib X-ray data showed no evidence for interactions—whether these be covalent or noncovalent—between neighboring BChl a molecules; however, the same analysis predicted the presence of extensive interactions between the chlorophyll molecules and the protein shell. Besides hydrophobic interactions, hydrogen bonding and coordination to the Mg ion in the BChl a molecule occurs. Over the years, the structure of the FMO protein from Prosthecochloris aestuarii has been refined (Matthews et al. Farnesyltransferase 1979; Tronrud et al. 1986) and recently a 1.3 Å diffraction dataset of the structure has been obtained (Tronrud et al. 2009). Fig. 1 a Representation of the FMO protein trimer of Prosthecochloris aestuarii showing the BChl a pigments surrounded by the protein envelope. b Protein envelope shell, consisting mainly of β sheets, enclosing the seven pigments. c View of the arrangement of the seven BChl a pigments. Identifier 3eoj [5] in the Brookhaven Protein Databank. Pictures are created with rasmol. The eighth BChl a is omitted for sake of clarity but can be created using the coordinates from Tronrud et al. (2009) In 1997, the crystal structure of FMO from Chlorobium tepidum was determined at a 2.2 Å resolution (Li et al. 1997). Similar to Prosthecochloris aestuarii (Fig.
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