Comparison of reaction centers from Rhodobacter sphaeroides and Rhodopseudomonas viridis: overall architecture and protein-pigment interactions.
about
Relationship between the oxidation potential and electron spin density of the primary electron donor in reaction centers from Rhodobacter sphaeroides.Targeted random mutagenesis to identify functionally important residues in the D2 protein of photosystem II in Synechocystis sp. strain PCC 6803Study of wild type and genetically modified reaction centers from Rhodobacter capsulatus: structural comparison with Rhodopseudomonas viridis and Rhodobacter sphaeroides.Protein modifications affecting triplet energy transfer in bacterial photosynthetic reaction centers.Metalloporphyrin mixed-valence π-cation radicals: [Fe(oxoOEC(•/2))(Cl)]2SbCl6, structure, magnetic properties, and near-IR spectra.Low frequency vibrational modes in proteins: changes induced by point-mutations in the protein-cofactor matrix of bacterial reaction centers.Site-specific and compensatory mutations imply unexpected pathways for proton delivery to the QB binding site of the photosynthetic reaction center.Efficient exchange of the primary quinone acceptor Q(A) in isolated reaction centers of Rhodopseudomonas viridis.Mixed-Valence Porphyrin π-Cation Radical Derivatives: Electrochemical Investigations.Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentansThe quinone-binding site in succinate-ubiquinone reductase from Escherichia coli. Quinone-binding domain and amino acid residues involved in quinone binding.Relationship between altered structure and photochemistry in mutant reaction centers in which bacteriochlorophyll replaces the photoactive bacteriopheophytin.Blue shifts in bacteriochlorophyll absorbance correlate with changed hydrogen bonding patterns in light-harvesting 2 mutants of Rhodobacter sphaeroides with alterations at alpha-Tyr-44 and alpha-Tyr-45.DCCD inhibits the reactions of the iron-sulfur protein in Rhodobacter sphaeroides chromatophores.The interaction of quinone and detergent with reaction centers of purple bacteria. I. Slow quinone exchange between reaction center micelles and pure detergent micelles.Crystallization and X-ray analysis of the reaction center from the thermophilic green bacterium Chloroflexus aurantiacus.NMR structural model of the interaction of herbicides with the photosynthetic reaction center from Rhodobacter sphaeroides.Synthesis, characterization and cation-induced dimerization of new aza-crown ether-appended metalloporphyrins.Primary and Higher Order Structure of the Reaction Center from the Purple Phototrophic Bacterium Blastochloris viridis: A Test for Native Mass Spectrometry.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.
P2860
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P2860
Comparison of reaction centers from Rhodobacter sphaeroides and Rhodopseudomonas viridis: overall architecture and protein-pigment interactions.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh-hant
name
Comparison of reaction centers ...... protein-pigment interactions.
@en
Comparison of reaction centers ...... protein-pigment interactions.
@nl
type
label
Comparison of reaction centers ...... protein-pigment interactions.
@en
Comparison of reaction centers ...... protein-pigment interactions.
@nl
prefLabel
Comparison of reaction centers ...... protein-pigment interactions.
@en
Comparison of reaction centers ...... protein-pigment interactions.
@nl
P2093
P356
P1433
P1476
Comparison of reaction centers ...... protein-pigment interactions.
@en
P2093
P304
P356
10.1021/BI00236A006
P407
P577
1991-06-01T00:00:00Z