Synechocystis sp. PCC

Masamoto, K. et al.. Identification of a gene required for cis-to-trans carotene isomerization in carotenogenesis of the cyanobacterium Synechocystis sp. PCC 6803, Plant Cell Physiol. 42, 1398, 2001. 

Rakhimberdieva, M. G., Y. V. Bolychevtseva, I. V. Elanskaya, and N. V. Karapetyan (2007a). Protein-protein interactions in carotenoid triggered quenching of phycobilisome fluorescence in Synechocystis sp. PCC 6803. FEBS Lett 581(13) 2429-2433. 

Ruch, S., P. Beyer et al. (2005). Retinal biosynthesis in eubacteria In vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803. Mol. Microbiol. 55(4) 1015-1024. 

Growth conditions of Synechocystis sp. PCC 6803 and subsequent isolation of thylakoid membranes were described in literature [8], From these membranes, PS I was extracted by dodecyl-B-D-maltoside treatment and purified by two successive HPLC steps, using first an anion exchange column (Poros 50 HQ, PerSeptive) and second a hydrophobic interaction column (Poros 20 Butyl, PerSeptive). The purification of trimeric PS I is described in detail in literature [9],... 

Appel, J., Phunpruch., S., Steinmuller, K. and Schulz, R. (2000) The bidirectional hydrogenase of Synechocystis sp PCC 6803 works as an electron valve during photosynthesis. Arch. Microbiol., 173, 333-8. 

Antal, T.K., Lindblad, P. 2005. Production of Hj by sulphur-deprived cells of the unicellular cyanobacteria Gloeocapsa alpicola and Synechocystis sp. PCC 6803 during dark incubation with methane or at various extracellular pH. J Appl Microbiol 98 114-120. 

Poluektov et al. used high-frequency time-resolved spin-polarised EPR spectroscopy of radical pairs to characterise quantitatively isotopically labelled quinine exchange in the PS I reaction centre of proteins.91 Intra-subunit interactions in the Fe-S cluster of PS I of Synechocystis sp. PCC 6803 were studied by using mutations and following the changes in stabilisation of the cluster by EPR spectroscopy.92... 

Fig. 4. Multiple sequence alignment of the precursors of seven cupredoxin sequences (hcpB through hcpG) and two BCB domains of the hcpA gene product (NDl and ND2) identified in the genome of an archaeon, Halohacterium sp. NRC-1, with that of halocyanin (Nhal) from Natronobacterium pharaonis and plastocyanin from a cyanobacterium, Synechocystis sp. PCC 6803.

Fig. 1. Ribbon drawing of the cyanobacterium Synechocystis sp. PCC 6803 Cu(II)-plastocyanin structure showing the secondary structure elements of the protein. The metal ion is represented as a sphere of arbitrary dimensions (Bertini et al., 2001b). The letters N, E, S, and W refer to the cardinal points. The so-called acidic patch present in the structure of plant plastocyanins is located in the E region.

Garcia-Dominguez, M., Reyes, J. C., and Florencio, F. J. (2000). Ntca represses transcription ofgi/A and giJB, genes that encode inhibitors of glutamine synthetase type I from Synechocystis sp., PCC 6803. Mol. Microbiol. 35, 1192-1201. 

Montesinos, M. L., Muro-Pastor, A. M., Herrero, A., and Flores, E. (1998). Ammonium/methylam-monium permeases of a cyanobacterium—Identification and analysis of three nitrogen-regulated amt genes in Synechocystis sp. PCC 6803. Biol. Chem. 273, 31463—31470. 

Appel, J. and Schulz, R. (1996). Sequence analysis of an operon of NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NADP(H)-dehydrogenase (complex I). Biochim. Biophys. Acta 1298,141-147. 

Howitt, C.A. and Vermaas, W.F.J. (1999). Subunits of the NAD(P)-reducing nickel-containing hydrogenase do not act as part of the type-1 NAD(P)H-dehydrogenase in the cyanobacterium Synechocystis sp. PCC 6803. In The Phototrophic Prokaryotes pp. 595-601. Edited by Peschek, G.A. Kluwer Academic/PIenum Publishers, New York, USA. 

WFJ Vermass, AW Rutherford and Flansson (1988) Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803 DonorD is a tyrosine residue in the D2 protein. Proc Nat Acad Sci, USA 85 8477-8481... 

Fig. 11. (A) Model for the homologous PsaA (and PsaB) subunits of photosystem I. Helices VIII and IX and the VIII-IX interhelical loop are shown inside the dashed ellipse (B) Amino-acid composition of the loop between helices VIII and IX in PsaA and PsaB. with the four cysteine residues numbered for Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803, respectively (separated by a slash). (C) A working model for the FeS-X domain consisting of a bundle of four a-helices (VIII and IX from PsaA and PsaB), the interhelical loops and FeS-X itself ligated to the four cysteine residues. Model in (C) is adapted from Rodday, Jun and Biggins (1993) Interaction of the Ff Fg-containing subunit with the photosystem I core heterodimer. Photosynthesis Res 36 3.

LB Smart, PV Warren, JH Golbeck and L McIntosh (1993) Mutational analysis of the structure and biogenesis of the photosystem I reaction center in the cyanobacterium Synechocystis sp. PCC 6803. Proc Nat Acad Sci, USA 90 1132-1136... 

Fig. 7. Picosecond kinetics of flash-induced absorbance changes at 432 and 380-390 nm in PS-1 core complex [PTOO-AqA,] isolated from Synechocystis sp. PCC 6803. Figure source Brettel and Vos (1998) Spectroscopic resolution of the picosecond reduction kineticsofthe secondary electron acceptor in photosystem I. FEBS Lett 447 316.

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