(Q44009163)

English

Tuning of the optical and electrochemical properties of the primary donor bacteriochlorophylls in the reaction centre from Rhodobacter sphaeroides: spectroscopy and structure

scientific article published in April 2002

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scholarly article

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Europe PubMed Central

PubMed publication ID

28 November 2017

Tuning of the optical and electrochemical properties of the primary donor bacteriochlorophylls in the reaction centre from Rhodobacter sphaeroides: spectroscopy and structure (English)

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

Rhodobacter sphaeroides

object named as

Rhodobacter sphaeroides

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based on heuristic

inferred from title

8

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Europe PubMed Central

PubMed publication ID

28 November 2017

Richard Cogdell

9

object named as

Richard J Cogdell

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28 November 2017

author name string

Diane Spiedel

1

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Europe PubMed Central

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28 November 2017

Aleksander W Roszak

2

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Europe PubMed Central

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28 November 2017

Kimberley McKendrick

3

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Europe PubMed Central

PubMed publication ID

28 November 2017

Katherine E McAuley

4

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

Paul K Fyfe

5

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

Eliane Nabedryk

6

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

Jacques Breton

7

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

Neil W Isaacs

10

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Europe PubMed Central

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28 November 2017

Michael R Jones

11

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28 November 2017

publication date

1 April 2002

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Europe PubMed Central

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28 November 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

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28 November 2017

1554

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Europe PubMed Central

PubMed publication ID

28 November 2017

1-2

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Europe PubMed Central

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28 November 2017

75-93

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors

1 reference

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Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides

1 reference

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Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions

1 reference

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Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides

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Nucleotide sequences of genes coding for photosynthetic reaction centers and light-harvesting proteins of Acidiphilium rubrum and related aerobic acidophilic bacteria.

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Mutations designed to modify the environment of the primary electron donor of the reaction center from Rhodobacter sphaeroides: phenylalanine to leucine at L167 and histidine to phenylalanine at L168.

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Relationship between rate and free energy difference for electron transfer from cytochrome c2 to the reaction center in Rhodobacter sphaeroides

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Specific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides

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Changes in primary donor hydrogen-bonding interactions in mutant reaction centers from Rhodobacter sphaeroides: identification of the vibrational frequencies of all the conjugated carbonyl groups

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Relationship between the oxidation potential of the bacteriochlorophyll dimer and electron transfer in photosynthetic reaction centers

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Correlation between multiple hydrogen bonding and alteration of the oxidation potential of the bacteriochlorophyll dimer of reaction centers from Rhodobacter sphaeroides.

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ENDOR studies of the primary donor cation radical in mutant reaction centers of Rhodobacter sphaeroides with altered hydrogen-bond interactions.

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Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution

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Low frequency vibrational modes in proteins: changes induced by point-mutations in the protein-cofactor matrix of bacterial reaction centers.

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7 January 2021

Site-specific mutagenesis of the reaction centre from Rhodobacter sphaeroides studied by Fourier transform Raman spectroscopy: mutations at tyrosine M210 do not affect the electronic structure of the primary donor.

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Oxidation-reduction potential of the ferro-ferricyanide system in buffer solutions

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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

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Structural details of an interaction between cardiolipin and an integral membrane protein

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Processing of X-ray diffraction data collected in oscillation mode

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AMoRe: an automated package for molecular replacement

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Refinement of macromolecular structures by the maximum-likelihood method

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7 January 2021

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Raster3D: photorealistic molecular graphics

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7 January 2021

Mutants of Rhodobacter sphaeroides lacking one or more pigment-protein complexes and complementation with reaction-centre, LH1, and LH2 genes

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7 January 2021

Construction and characterization of a mutant of Rhodobacter sphaeroides with the reaction center as the sole pigment-protein complex

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7 January 2021

Energies and kinetics of radical pairs involving bacteriochlorophyll and bacteriopheophytin in bacterial reaction centers

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7 January 2021

Fourier transform infrared study of the primary electron donor in chromatophores of Rhodobacter sphaeroides with reaction centers genetically modified at residues M160 and L131

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7 January 2021

Heterodimeric versus homodimeric structure of the primary electron donor in Rhodobacter sphaeroides reaction centers genetically modified at position M202

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7 January 2021

A new infrared electronic transition of the oxidized primary electron donor in bacterial reaction centers: a way to assess resonance interactions between the bacteriochlorophylls

1 reference

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7 January 2021

Probing the primary donor environment in the histidineM200-->leucine and histidineL173-->leucine heterodimer mutants of Rhodobacter capsulatus by light-induced Fourier transform infrared difference spectroscopy

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A solution for the best rotation to relate two sets of vectors

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Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center

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X-ray crystal structure of the YM210W mutant reaction centre from Rhodobacter sphaeroides

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Femtosecond processes in proteins

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Electrochromic detection of a coherent component in the formation of the charge pair P(+)H(L)(-) in bacterial reaction centers

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Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions

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Effects of hydrogen bonds on the redox potential and electronic structure of the bacterial primary electron donor

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An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre

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Kinetics and free energy gaps of electron-transfer reactions in Rhodobacter sphaeroides reaction centers

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Tyrosine 162 of the photosynthetic reaction center L-subunit plays a critical role in the cytochrome c2 mediated rereduction of the photooxidized bacteriochlorophyll dimer in Rhodobacter sphaeroides. 2. Quantitative kinetic analysis.

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Effects of mutations near the bacteriochlorophylls in reaction centers from Rhodobacter sphaeroides

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Comparative study of reaction centers from photosynthetic purple bacteria: electron paramagnetic resonance and electron nuclear double resonance spectroscopy.

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Relationship between the oxidation potential and electron spin density of the primary electron donor in reaction centers from Rhodobacter sphaeroides

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Two distinct conformations of the primary electron donor in reaction centers from Rhodobacter sphaeroides revealed by ENDOR/TRIPLE-spectroscopy

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Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer

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Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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Errors in protein structures

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PROCHECK: a program to check the stereochemical quality of protein structures

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10.1016/S0005-2728(02)00215-3

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Europe PubMed Central

PubMed publication ID

28 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

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