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3.E.2.1.1
Photosynthetic reaction center (RC).  Chromatophores containing the RC and light harvesting complex, LH1, can interface with a conducting support to allow capture and conversion of solar energy as an alternative fuel source (Harrold et al. 2013). This RC may catalyze transmembrane electron transfer, as for members of TC class 5 (Khatypov et al. 2017). Cytochrome bc1 and the reaction centre complex are in proximity in live Rhodobacter sphaeroides cells (Vasilev et al. 2021).  Dipyridamole (DIP) alters the efficiency of energy transfer from the light-harvesting complex LH2 to the LH1-reaction center core complex and to produce the long-wavelength ("red") shift of the absorption band of light-harvesting bacteriochlorophyll molecules in the IR spectral region at 840-900 nm (Knox et al. 2022). This shift is associated with the membrane transition to the energized state. DIP reduces the photooxidized bacteriochlorophyll of the reaction center, which accelerated electron flow along the electron transport chain, thereby stimulating generation of the transmembrane potential on the chromatophore membrane (Knox et al. 2022).  Tools for analyzing protonation states and for tracing proton transfer pathways have been developed with examples from the Rb. sphaeroides photosynthetic reaction centers (Wei et al. 2023).

Accession Number:P0C0Y9
Protein Name:RCEM aka PUFM
Length:308
Molecular Weight:34509.00
Species:Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides) [1063]
Number of TMSs:5
Location1 / Topology2 / Orientation3: Cellular chromatophore membrane1 / Multi-pass membrane protein2
Substrate

Cross database links:

Pfam: PF00124   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0030077 C:plasma membrane light-harvesting complex
GO:0042717 C:plasma membrane-derived chromatophore membrane
GO:0042314 F:bacteriochlorophyll binding
GO:0045156 F:electron transporter, transferring electron...
GO:0046872 F:metal ion binding
GO:0009772 P:photosynthetic electron transport in photos...
GO:0018298 P:protein-chromophore linkage
GO:0006810 P:transport

References (7)

[1] “Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides.”  Williams J.C.et.al.   16593385
[2] “Towards the understanding of the function of Rb sphaeroides Y wild type reaction center: gene cloning, protein and detergent structures in the three-dimensional crystals.”  Arnoux B.et.al.   2126457
[3] “Primary structure of the L subunit of the reaction center from Rhodopseudomonas sphaeroides.”  Williams J.C.et.al.   6095283
[4] “Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides.”  Chang C.-H.et.al.   2036404
[5] “Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.”  Allen J.P.et.al.   3054889
[6] “Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits.”  Allen J.P.et.al.   2819866
[7] “Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal.”  McAuley-Hecht K.E.et.al.   9537989
Structure:
1AIG   1AIJ   1DS8   1DV3   1DV6   1E14   1E6D   1F6N   1FNP   1FNQ   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAEYQNIFSQ VQVRGPADLG MTEDVNLANR SGVGPFSTLL GWFGNAQLGP IYLGSLGVLS 
61:	LFSGLMWFFT IGIWFWYQAG WNPAVFLRDL FFFSLEPPAP EYGLSFAAPL KEGGLWLIAS 
121:	FFMFVAVWSW WGRTYLRAQA LGMGKHTAWA FLSAIWLWMV LGFIRPILMG SWSEAVPYGI 
181:	FSHLDWTNNF SLVHGNLFYN PFHGLSIAFL YGSALLFAMH GATILAVSRF GGERELEQIA 
241:	DRGTAAERAA LFWRWTMGFN ATMEGIHRWA IWMAVLVTLT GGIGILLSGT VVDNWYVWGQ 
301:	NHGMAPLN