Publications

• Three-dimensional structure of cyanobacterial photosystem I at 2.5 A resolution.

  Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N.

  Life on Earth depends on photosynthesis, the conversion of light energy from the Sun to chemical energy. In plants, green algae and cyanobacteria, this process is driven by the cooperation of two large protein-cofactor complexes, photosystems I and II, which are located in the thylakoid photosynth ... >> More

  Life on Earth depends on photosynthesis, the conversion of light energy from the Sun to chemical energy. In plants, green algae and cyanobacteria, this process is driven by the cooperation of two large protein-cofactor complexes, photosystems I and II, which are located in the thylakoid photosynthetic membranes. The crystal structure of photosystem I from the thermophilic cyanobacterium Synechococcus elongatus described here provides a picture at atomic detail of 12 protein subunits and 127 cofactors comprising 96 chlorophylls, 2 phylloquinones, 3 Fe4S4 clusters, 22 carotenoids, 4 lipids, a putative Ca2+ ion and 201 water molecules. The structural information on the proteins and cofactors and their interactions provides a basis for understanding how the high efficiency of photosystem I in light capturing and electron transfer is achieved. << Less

  Nature 411:909-917(2001) [PubMed] [EuropePMC]

• Subunit composition of Photosystem I complex that catalyzes light-dependent transfer of electrons from plastocyanin to ferredoxin.

  Takabe T., Iwasaki Y., Hibino T., Ando T.

  The PSI core complex prepared from cucumber cotyledons, which contains 80 chlorophylls per reaction center (P700) and eight polypeptides with apparent molecular masses of 65/63, 20, 19.5, 18.5, 17.5, 7.6, and 5.8 kDa, has been shown to catalyze the light-dependent transfer of electrons from plasto ... >> More

  The PSI core complex prepared from cucumber cotyledons, which contains 80 chlorophylls per reaction center (P700) and eight polypeptides with apparent molecular masses of 65/63, 20, 19.5, 18.5, 17.5, 7.6, and 5.8 kDa, has been shown to catalyze the light-dependent transfer of electrons from plastocyanin to ferredoxin. The "native" PSI complex, which contains more than fifteen polypeptides and 120 chlorophylls per P700, did not show higher activity. Any attempt to deplete subunit(s) of the core complex decreased its activity. These results suggest that in addition to light-harvesting chlorophyll a/b protein complexes, several genes of psaA-psaK, which have been proposed as components of PSI complex, are not involved in the activity of PSI complex. It was also found that the amount of 18.5-kDa polypeptide in the PSI complex affects the activity: when this polypeptide was largely depleted, the complex was almost inactive. The inactivation was due to inhibition of electron transfer from plastocyanin to photooxidized P700. Chemical cross-linking and N-terminal amino acid sequencing experiments indicated that the 18.5-kDa polypeptide is the plastocyanin-docking protein and the psaF gene product. The function of the psaF gene product was discussed. << Less

  J Biochem 110:622-627(1991) [PubMed] [EuropePMC]

• PHOTOSYSTEM I: Function and Physiology.

  Chitnis P.R.

  Photosystem I is the light-driven plastocyanin-ferredoxin oxidoreductase in the thylakoid membranes of cyanobacteria and chloroplasts. In recent years, sophisticated spectroscopy, molecular genetics, and biochemistry have been used to understand the light conversion and electron transport function ... >> More

  Photosystem I is the light-driven plastocyanin-ferredoxin oxidoreductase in the thylakoid membranes of cyanobacteria and chloroplasts. In recent years, sophisticated spectroscopy, molecular genetics, and biochemistry have been used to understand the light conversion and electron transport functions of photosystem I. The light-harvesting complexes and internal antenna of photosystem I absorb photons and transfer the excitation energy to P700, the primary electron donor. The subsequent charge separation and electron transport leads to the reduction of ferredoxin. The photosystem I proteins are responsible for the precise arrangement of cofactors and determine redox properties of the electron transfer centers. With the availability of genomic information and the structure of photosystem I, one can now probe the functions of photosystem I proteins and cofactors. The strong reductant produced by photosystem I has a central role in chloroplast metabolism, and thus photosystem I has a critical role in the metabolic networks and physiological responses in plants. << Less

  Annu Rev Plant Physiol Plant Mol Biol 52:593-626(2001) [PubMed] [EuropePMC]

• Localization of two phylloquinones, QK and QK', in an improved electron density map of photosystem I at 4-A resolution.

  Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T., Saenger W.

  An improved electron density map of photosystem I from Synechococcus elongatus calculated at 4-A resolution for the first time reveals a second phylloquinone molecule and thereby completes the set of cofactors constituting the electron transfer system of this iron-sulfur type photosynthetic reacti ... >> More

  An improved electron density map of photosystem I from Synechococcus elongatus calculated at 4-A resolution for the first time reveals a second phylloquinone molecule and thereby completes the set of cofactors constituting the electron transfer system of this iron-sulfur type photosynthetic reaction center: six chlorophyll a, two phylloquinones, and three Fe4S4 clusters. The location of the newly identified phylloquinone pair, the individual plane orientations of these molecules, and the resulting distances to other cofactors of the electron transfer system are discussed and compared with those determined by magnetic resonance techniques. << Less

  J. Biol. Chem. 274:7361-7367(1999) [PubMed] [EuropePMC]

• Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and PsaE.

  Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T., Saenger W.

  An improved electron density map of photosystem I (PSI) calculated at 4-A resolution yields a more detailed structural model of the stromal subunits PsaC, PsaD, and PsaE than previously reported. The NMR structure of the subunit PsaE of PSI from Synechococcus sp. PCC7002 (Falzone, C. J., Kao, Y.-H ... >> More

  An improved electron density map of photosystem I (PSI) calculated at 4-A resolution yields a more detailed structural model of the stromal subunits PsaC, PsaD, and PsaE than previously reported. The NMR structure of the subunit PsaE of PSI from Synechococcus sp. PCC7002 (Falzone, C. J., Kao, Y.-H., Zhao, J., Bryant, D. A., and Lecomte, J. T. J. (1994) Biochemistry 33, 6052-6062) has been used as a model to interpret the region of the electron density map corresponding to this subunit. The spatial orientation with respect to other subunits is described as well as the possible interactions between the stromal subunits. A first model of PsaD consisting of a four-stranded beta-sheet and an alpha-helix is suggested, indicating that this subunit partly shields PsaC from the stromal side. In addition to the improvements on the stromal subunits, the structural model of the membrane-integral region of PSI is also extended. The current electron density map allows the identification of the N and C termini of the subunits PsaA and PsaB. The 11-transmembrane alpha-helices of these subunits can now be assigned uniquely to the hydrophobic segments identified by hydrophobicity analyses. << Less

  J. Biol. Chem. 274:7351-7360(1999) [PubMed] [EuropePMC]

• Photosystem I at 4-A resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system.

  Krauss N., Schubert W.-D., Klukas O., Fromme P., Witt H.T., Saenger W.

  The 4 A X-ray structure model of trimeric photosystem I of the cyanobacterium Synechococcus elongatus reveals 31 transmembrane, nine surface and three stromal alpha-helices per monomer, assigned to the 11 protein subunits: PsaA and PsaB are related by a pseudo two-fold axis normal to the membrane ... >> More

  The 4 A X-ray structure model of trimeric photosystem I of the cyanobacterium Synechococcus elongatus reveals 31 transmembrane, nine surface and three stromal alpha-helices per monomer, assigned to the 11 protein subunits: PsaA and PsaB are related by a pseudo two-fold axis normal to the membrane plane, along which the electron transfer pigments are arranged. 65 antenna chlorophyll a (Chl a) molecules separated by < or = 16 A form an oval, clustered net continuous with the electron transfer chain through the second and third Chl a pairs of the electron transfer system. This suggests a dual role for these Chl a both in excitation energy and electron transfer. The architecture of the protein core indicates quinone and iron-sulphur type reaction centres to have a common ancestor. << Less

  Nat. Struct. Biol. 3:965-973(1996) [PubMed] [EuropePMC]