The position of cytochrome b(559) relative to Q(A) in photosystem II studied by electron-electron double resonance (ELDOR).

No abstract is available for this paper.

• Publication year

  2000

• Venue

  Biochimica et Biophysica Acta

• Publication date

  2000-11-20

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1016/S0005-2728(00)00199-7PMID 11106773
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• On the structure and function of cytochrome b-559

  2004cited by this paper
• The role of cytochrome b559 and tyrosineD in protection against photoinhibition during in vivo photoactivation of photosystem II

  1999cited by this paper
• Relative positions of electron transfer components in Photosystem II studied by ‘2+1’ pulsed electron paramagnetic resonance: YD and QA

  1999cited by this paper
• Restoration of the high-potential form of cytochrome b559 of photosystem II occurs via a two-step mechanism under illumination in the presence of manganese ions

  1999cited by this paper
• Carotenoid oxidation in photosystem II.

  1999cited by this paper
• The pulsed electron–electron double resonance and “2+1” electron spin echo study of the oriented oxygen-evolving and Mn-depleted preparations of photosystem II

  1998cited by this paper
• Cytochrome b559 of photosystem II.

  1998cited by this paper
• Determination of distances from tyrosine D to QA and chlorophyllZ in photosystem II studied by '2+1' pulsed EPR

  1998cited by this paper
• The distance between P680 and QA in Photosystem II determined by ESEEM spectroscopy

  1997cited by this paper
• Photosystem I of Synechococcus elongatus at 4 A resolution: comprehensive structure analysis.

  1997cited by this paper
• The distances from tyrosine D to redox-active components on the donor side of Photosystem II determined by pulsed electron-electron double resonance

  1996cited by this paper
• Form and function of cytochrome b-559

  1996cited by this paper
• Proximity of the manganese cluster of photosystem II to the redox-active tyrosine YZ.

  1995cited by this paper
• Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II.

  1995cited by this paper
• Cyanide binding at the non-heme Fe2+ of the iron-quinone complex of photosystem II: at high concentrations, cyanide converts the Fe2+ from high (S = 2) to low (S = 0) spin.

  1994cited by this paper
• Topography of the heme prosthetic group of cytochrome b-559 in the photosystem II reaction center.

  1994cited by this paper
• Composition and function of cytochrome b559 in reaction centers of photosystem II of green plants

  1994cited by this paper
• Location of chlorophyllZ in photosystem II.

  1994cited by this paper
• Distance between tyrosines Z+ and D+ in plant Photosystem II as determined by pulsed EPR

  1994cited by this paper
• Reevaluation of the stoichiometry of cytochrome b559 in photosystem II and thylakoid membranes.

  1992cited by this paper
• Location of D+ and distribution of surface charges in Photosystem II

  1990cited by this paper
• Selection of dipolar interaction by the “2 + 1” pulse train ESE

  1989cited by this paper
• Stoichiometry of cytochrome b-559 in Photosystem II

  1989cited by this paper
• Visualization of antibody binding to the photosynthetic membrane: the transmembrane orientation of cytochrome b-559.

  1989cited by this paper
• Directed mutagenesis indicates that the donor to P+680 in photosystem II is tyrosine-161 of the D1 polypeptide.

  1988cited by this paper
• Cytochrome b-559 may function to protect photosystem II from photoinhibition.

  1988cited by this paper
• Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: Donor D is a tyrosine residue in the D2 protein.

  1988cited by this paper
• Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II

  1988cited by this paper
• Refined purification and further characterization of oxygen-evolving and Tris-treated Photosystem II particles from the thermophilic Cyanobacterium synechococcus sp.

  1988cited by this paper
• Thylakoid membrane protein topography: transmembrane orientation of the chloroplast cytochrome b-559 psbE gene product.

  1988cited by this paper
• Isolation and characterization of an oxygen-evolving Photosystem II reaction center core preparation and a 28 kDa Chl-a-binding protein

  1987cited by this paper
• Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions.

  1987cited by this paper
• Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

  1985cited by this paper
• Axial ligands of chloroplast cytochrome b-559: identification and requirement for a heme-cross-linked polypeptide structure.

  1985cited by this paper
• Orientation of EPR signals arising from components in Photosystem II membranes

  1985cited by this paper
• A new EPR signal attributed to the primary plastosemiquinone acceptor in Photosystem II

  1984cited by this paper
• Electron-electron double resonance in electron spin echo: Model biradical systems and the sensitized photolysis of decalin

  1984cited by this paper
• The orientation of the magnetic axes of membrane-bound iron-sulfur clusters and a cytochrome b-559 in the green halophilic alga Dunaliella parva

  1983cited by this paper
• Inactivation of Photosynthetic Oxygen Evolution and Concomitant Release of Three Polypeptides in the Photosystem II Particles of Spinach Chloroplasts

  1982cited by this paper
• EPR signals and orientation of cytochromes in the spinach chloroplast thylakoid membrane

  1982cited by this paper
• Interaction between the intermediary electron acceptor (pheophytin) and a possible plastoquinone-iron complex in photosystem II reaction centers.

  1980cited by this paper

• PELDOR in Photo- and Radiation Chemistry

  2018cites this paper
• Pulsed Electron–Electron Double Resonance: Nanoscale Distance Measurement in the Biological, Materials and Chemical Sciences

  2018cites this paper
• Electron Transfer and Structure of Plant Photosystem II

  2012cites this paper
• Metal-Based Spin Labeling for Distance Determination

  2012cites this paper
• 1.20 Electron Magnetic Resonance

  2012cites this paper
• Structural information from orientationally selective DEER spectroscopy.

  2009cites this paper
• Pulsed electron–electron double resonance (PELDOR) as EPR spectroscopy in nanometre range

  2008cites this paper
• Distance Measurements in Photosynthetic Reaction Centers by Pulsed EPR

  2008cites this paper
• Long-rangedistancedeterminations in biomacromoleculesbyEPRspectroscopy

  2007cites this paper
• Long-range distance determinations in biomacromolecules by EPR spectroscopy

  2007cites this paper
• ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY

  2006cites this paper
• Configuration of Electron Transfer Components Studied by EPR Spectroscopy

  2005cites this paper
• Characteristic features of the interaction between Fe(II) cations and the donor side of the manganese-depleted photosystem II

  2005cites this paper
• Electron-Electron Double Resonance

  2005cites this paper
• Visualization of distance distribution from pulsed double electron-electron resonance data

  2004cites this paper
• Structural analysis of three-spin systems of photosystem II by PELDOR

  2003cites this paper
• Heterogeneity of photosystem II as it occurs in domain specific regions of the thylakoid membrane of spinach (spinacia oleracia L.)

  2002cites this paper
• The heart of photosynthesis in glorious 3

  2001cites this paper
• The heart of photosynthesis in glorious 3D.

  2001cites this paper
• Beta-carotene redox reactions in photosystem II: electron transfer pathway.

  2001cites this paper
• Pulsed electron paramagnetic resonance methods for macromolecular structure determination.

  2001cites this paper