Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution

Jordan, Patrick; Fromme, Petra; Witt, H. T.; Klukas, Olaf; Saenger, Wolfram; Krauß, Norbert

doi:10.1038/35082000

Cited by 2,415 publications

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“…However, previous observations of a high degree of similarity between PSI core complexes from different organisms (an impressing similarity was shown recently for PSI from the cyanobacterium T. elongatus 8 and higher plants 45 ), together with our observation of spectral similarities between C700 and cyanobacterial C703 and C708 pools indicate that C700 is located in the PSI core. The number of ∼5 Chls in C700, which is slightly more than the number of Chls in C703 and C708, suggests further that it may be contributed by two to three Chl dimers (or a dimer plus trimer), one to two of them not having a counterpart in cyanobacterial PSI.…”

Section: Discussionsupporting

confidence: 64%

Characterization of Low-Energy Chlorophylls in the PSI-LHCI Supercomplex from Chlamydomonas reinhardtii. A Site-Selective Fluorescence Study

et al. 2005

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Almost all photosystem I (PSI) complexes from oxygenic photosynthetic organisms contain chlorophylls that absorb at longer wavelength than that of the primary electron donor P700. We demonstrate here that the low-energy pool of chlorophylls in the PSI-LHCI complex from the green alga Chlamydomonas reinhardtii, containing five to six pigments, is significantly blue-shifted (A max at 700 nm at 4 K) compared to that in the PSI core preparations from several species of cyanobacteria and in PSI-LHCI particles from higher plants. This makes them almost isoenergetic with the primary donor. However, they keep the other characteristic features of "red" chlorophylls: clear spectral separation from the bulk chlorophylls, big Stokes shift revealing pronounced electron-phonon coupling, and large homogeneous and inhomogeneous broadening of ∼170 and ∼310 cm -1 , respectively.

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Section: Discussionsupporting

confidence: 64%

Characterization of Low-Energy Chlorophylls in the PSI-LHCI Supercomplex from Chlamydomonas reinhardtii. A Site-Selective Fluorescence Study

et al. 2005

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“…It is unlikely that the PsaA/B heterodimer can have additional binding sites for significantly more Chl molecules than the 90 found in other cyanobacterial strains, since high resolution X-ray crystallography has shown the PS I complex to be almost filled with chlorophyll molecules which are spaced and tilted in an optimal fashion for efficient energy transfer (Jordan et al 2001). This would imply the necessity for one or more additional chlorophyll bearing polypeptides on which the superfluous Chl molecules could be organised.…”

Section: Electron Microscopymentioning

confidence: 98%

“…PS I complexes from a whole range of cyanobacterial strains have been studied extensively in the past years. The structure of trimeric PS I from Synechococcus elongatus has been resolved at 2.5 Å by X-ray analysis, making cyanobacterial PS I the first reaction centre of oxygenic photosynthesis for which a high resolution structure is available (Jordan et al 2001).…”

Section: Introductionmentioning

confidence: 99%

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Mangels

Kruip

Berry

et al. 2002

Photosynthesis Research

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Photosystem I from the unusual cyanobacterium Gloeobacter violaceus Mangels, D.; Kruip, J.; Berry, S.; Rögner, M.; Boekema, E.J.; Koenig, F. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Key words: antenna system, electron microscopy, fluorescence, light harvesting, photosynthesis, plasma membrane AbstractPhotosystem I (PS I) from the primitive cyanobacterium Gloeobacter violaceus has been purified and characterised. Despite the fact that the isolated complexes have the same subunit composition as complexes from other cyanobacteria, the amplitude of flash-induced absorption difference spectra indicates a much bigger antenna size with about 150 chlorophylls per P700 as opposed to the usual 90. Image analysis of the PS I preparation from Gloeobacter reveals that the PS I particles exist both in a trimeric and in a monomeric form and that their size and shape closely resembles other cyanobacterial PS I particles. However, the complexes exhibit a higher molecular weight as could be shown by gel filtration. The preparation contains novel polypeptides not related to known Photosystem I subunits. The N-terminal sequence of one of those polypeptides has been determined and reveals no homology to known or hypothetical proteins. Immunoblotting shows a cross-reaction of three of the polypeptide bands with an antibody raised against the major LHC from the diatom Cyclotella cryptica. Electron microscopy reveals a novel T-shaped complex which has never been observed in any other cyanobacterial PS I preparation. 77 K spectra of purified PS I show an extreme blue-shift of the fluorescence emission, indicating an unusual organisation of the PS I antenna system in Gloeobacter.Abbreviations: PS -photosystem; Chl -chlorophyll; DM -dodecyl-β-D-maltoside; ECL -enhanced chemiluminescence; HPLC -high performance liquid chromatography; IEC -ion exchange chromatography; GF -gel filtration; LHC I -light harvesting complex associated with Photosystem I; P700 -primary electron donor of photosystem I; SDS -sodium dodecyl sulfate; SQDG -sulfoquinovosyl diacylglycerol; PAGE -polyacrylamide gel electrophoresis; F760 (F730) -fluorescence band with maximal emission at 760 nm (730 nm)

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“…Although there appears to be a high degree of symmetry in the ET chain in PS I (9,10), this symmetry does not extend to P700, the primary electron donor. It is therefore likely † This work was supported by start-up funds, a quality improvement grant, and a research initiation grant to G.H.…”

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confidence: 90%

Mutation Induced Modulation of Hydrogen Bonding to P700 Studied Using FTIR Difference Spectroscopy

et al. 2003

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Site-directed mutagenesis in combination with Fourier transform infrared difference spectroscopy has been used to study how hydrogen bonding modulates the electronic and physical organization of P700, the primary electron donor in photosystem I. Wild-type PS I particles from Chlamydomonas reinhardtii and a mutant in which ThrA739 is changed to alanine [TA(A739) mutant] were studied. ThrA739 is thought to provide a hydrogen bond to the chlorophyll-a′ molecule of P700 (the two chlorophylls of P700 (P700 + ) will be called P A and P B (P A + and P B + )). The mutation considerably alters the (P700 + -P700) FTIR difference spectra. However, we were able to describe all of the mutation induced changes in the difference spectra in terms of difference band assignments that were proposed recently (Hastings, G., Ramesh, V. M., Wang, R., Sivakumar, V. and Webber, A. (2001) Biochemistry 40, 12943-12949). Upon comparison of mutant and wild type (P700 + -P700) FTIR difference spectra, it is shown that (1) the 13 3 ester carbonyl modes of P A and P B are unaltered upon mutation of ThrA739 to alanine. (2) The 13 3 ester carbonyl modes of P A + /P B + upshift/downshift upon mutation. These oppositely directed shifts indicate that the mutation modifies the charge distribution over the pigments in the P700 + state, with charge on P B being relocated onto P A . We also show that the 13 1 keto carbonyl mode of P B /P B + is unaltered/ downshifted upon mutation, as is expected for the above-described mutation induced charge redistribution in P700 + . Although the 13 3 ester carbonyl modes of the chlorophylls of P700 in the ground state are unaltered upon mutation, the 13 1 keto carbonyl mode of P A upshifts upon mutation, as does the 13 1 keto carbonyl mode of P A + . For P700 in the ground state, bands that we associate with HisA676/HisB656 upshift/downshift upon mutation. For the P700 + state, bands that we associate with HisA676/HisB656 also upshift/downshift upon mutation. These observations are also consistent with the notion that the mutation leads to the charge on P B + being relocated onto P A + . In addition, we suggest that a hydrogen bond to the 13 1 keto carbonyl of P A is still present in the TA(A739) mutant, probably mediated through an introduced water molecule.

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Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution

Cited by 2,415 publications

References 48 publications

Characterization of Low-Energy Chlorophylls in the PSI-LHCI Supercomplex from Chlamydomonas reinhardtii. A Site-Selective Fluorescence Study

Characterization of Low-Energy Chlorophylls in the PSI-LHCI Supercomplex from Chlamydomonas reinhardtii. A Site-Selective Fluorescence Study

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Mutation Induced Modulation of Hydrogen Bonding to P700 Studied Using FTIR Difference Spectroscopy

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