Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.
about
Interactions between lipids and bacterial reaction centers determined by protein crystallographyProtein engineering of cytochrome b562 for quinone binding and light-induced electron transfer.Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species.Pathway of proton transfer in bacterial reaction centers: replacement of serine-L223 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone.Conformationally controlled pK-switching in membrane proteins: one more mechanism specific to the enzyme catalysis?Correlation of paramagnetic states and molecular structure in bacterial photosynthetic reaction centers: the symmetry of the primary electron donor in Rhodopseudomonas viridis and Rhodobacter sphaeroides R-26.Study of wild type and genetically modified reaction centers from Rhodobacter capsulatus: structural comparison with Rhodopseudomonas viridis and Rhodobacter sphaeroides.Electronic structure of Q-A in reaction centers from Rhodobacter sphaeroides. I. Electron paramagnetic resonance in single crystals.Photosynthetic apparatus in Roseateles depolymerans 61A is transcriptionally induced by carbon limitation.Electron paramagnetic resonance investigation of photosynthetic reaction centers from Rhodobacter sphaeroides R-26 in which Fe2+ was replaced by Cu2+. Determination of hyperfine interactions and exchange and dipole-dipole interactions between Cu2+ aSpin-lattice relaxation of coupled metal-radical spin-dimers in proteins: application to Fe(2+)-cofactor (Q(A)(-.), Q(B)(-.), phi(-.)) dimers in reaction centers from photosynthetic bacteria.Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover.How does cytochrome oxidase pump protons?Pathway of proton transfer in bacterial reaction centers: second-site mutation Asn-M44-->Asp restores electron and proton transfer in reaction centers from the photosynthetically deficient Asp-L213-->Asn mutant of Rhodobacter sphaeroides.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.The smallest membrane anchoring subunit (QPs3) of bovine heart mitochondrial succinate-ubiquinone reductase. Cloning, sequencing, topology, and Q-binding domain.Coupling of cytochrome and quinone turnovers in the photocycle of reaction centers from the photosynthetic bacterium Rhodobacter sphaeroides.Plasmon waveguide resonance spectroscopic evidence for differential binding of oxidized and reduced Rhodobacter capsulatus cytochrome c2 to the cytochrome bc1 complex mediated by the conformation of the Rieske iron-sulfur protein.The semiquinone-iron complex of photosystem II: structural insights from ESR and theoretical simulation; evidence that the native ligand to the non-heme iron is carbonateLocations of Arg-82, Asp-85, and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundariesPotentiation of proton transfer function by electrostatic interactions in photosynthetic reaction centers from Rhodobacter sphaeroides: First results from site-directed mutation of the H subunit.Photochemical charge separation in photosynthetic reaction centers.The fe2+ site of photosynthetic reaction centers probed by multiple scattering x-ray absorption fine structure spectroscopy: improving structure resolution in dry matricesDirected mutagenesis of the Rhodobacter capsulatus puhA gene and orf 214: pleiotropic effects on photosynthetic reaction center and light-harvesting 1 complexes.Asymmetric binding of the 1- and 4-C=O groups of QA in Rhodobacter sphaeroides R26 reaction centres monitored by Fourier transform infra-red spectroscopy using site-specific isotopically labelled ubiquinone-10Probing the secondary quinone (QB) environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy.Highly oriented photosynthetic reaction centers generate a proton gradient in synthetic protocells.Modeling alpha-helical transmembrane domains: the calculation and use of substitution tables for lipid-facing residues.Low-temperature pulsed EPR study at 34 GHz of the triplet states of the primary electron Donor P865 and the carotenoid in native and mutant bacterial reaction centers of Rhodobacter sphaeroides.Design, synthesis and properties of synthetic chlorophyll proteins.Structure of the plant alternative oxidase. Site-directed mutagenesis provides new information on the active site and membrane topology.Cytochrome b6 arginine 214 of Synechococcus sp. PCC 7002, a key residue for quinone-reductase site function and turnover of the cytochrome bf complex.Inhibitor probes of the quinone binding sites of mammalian complex II and Escherichia coli fumarate reductase.Characterization by FTIR spectroscopy of the photoreduction of the primary quinone acceptor QA in photosystem II.Temperature dependence of the electrogenic reaction in the QB site of the Rhodobacter sphaeroides photosynthetic reaction center: the QA − QB →QA QB − transitionElectrogenesis associated with proton transfer in the reaction center protein of the purple bacterium Rhodobacter sphaeroides
P2860
Q27639471-EF17102C-6CC1-4951-8C18-A256203DB5B5Q33580348-D8A14A16-3816-48B9-B93A-D64ABECB2EB3Q33678700-077598A8-1F91-4FF2-AD37-DBF5511D9EE5Q33773605-B62231CA-2BED-45AB-9911-DAA43DEC8D35Q33801133-B54DCFA0-505D-4941-A882-53AB6BBCB41EQ33860407-E8B71A3A-E06D-4863-AAAC-20127CD14998Q34019516-A2773D54-6093-4928-B7BC-07AAB63477F8Q34046911-5F4E24C9-0A90-40CF-9DA2-0C7103437864Q34052552-36FA8A7D-4C70-4E30-AB91-879B9F1C7356Q34126170-304EE8A9-49EE-478B-9207-CD99FE032931Q34179061-9E1165E9-12D0-46BE-AFE4-1004D22B874FQ34300646-CBE4FA4D-0DAA-47EE-87B5-ADEA4D789804Q36079933-5B9B50B1-0A80-4216-B935-4F02BC4BB30EQ36101981-D7B0706B-0C36-43E0-B0F1-4D649EA76522Q36562326-7CB50E37-C649-413E-8901-793D4FA43B4CQ36592803-CFD5F148-185A-461A-B3D2-CA7B3AAA8CEFQ36869404-691BBA41-C0AA-49A0-93E8-8133C7084CF6Q36875529-0B5D79C0-F4E1-4481-8134-F23E6EAE9380Q36932573-5870BA1B-EF76-4931-8B8F-DEA863B01BABQ37373411-0F79DC8D-1F5E-4EFE-9C5A-C9EF336E77EFQ37599688-D84D9A25-DE04-4A3C-B2CE-144741FAF9C0Q37669865-41372B36-DCCB-446A-BDA4-1C8D6E56AFEEQ38771126-8E92C61C-5507-4856-B311-72D2D707A1F8Q39594202-C94C142B-EEE9-4874-A5D2-01E48DF1AFFBQ39841039-A5DF335C-A389-4655-8163-D82C6DC039E4Q40793954-64A00196-5926-4DA2-9DEB-969245FD629BQ42136189-68111C01-5986-4552-9C5B-2C5EB446FCD6Q42291312-FDBC0BC1-8236-4FF6-A155-CA28196B9FB4Q42842499-75269F51-C06F-4F7C-B6E9-1B1DBB7B6F8AQ42966124-08E76579-D180-478C-9132-343A9B878B3AQ43628330-06E0C8E4-2A1E-460D-95A0-AAFB2A3DAC68Q43792257-F70ED4DD-D9D7-418C-A2A2-8E74AC7B100BQ45211574-CF94FC0F-DCBE-4F04-B597-70BE76A3605DQ46040379-1A72D248-CAFC-4295-BDF0-74C5959D94A4Q47969948-A84B4A8B-BB29-4E74-91BC-15E6FD787F0DQ58047838-596AD42C-4BA9-44A6-A03F-946CE9C120E0Q58047878-E7D02F1B-E1D0-43E0-A17D-5D7E1179D696
P2860
Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.
description
1988 nî lūn-bûn
@nan
1988 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
name
Structure of the reaction cent ...... inones and Fe2+) interactions.
@ast
Structure of the reaction cent ...... inones and Fe2+) interactions.
@en
type
label
Structure of the reaction cent ...... inones and Fe2+) interactions.
@ast
Structure of the reaction cent ...... inones and Fe2+) interactions.
@en
prefLabel
Structure of the reaction cent ...... inones and Fe2+) interactions.
@ast
Structure of the reaction cent ...... inones and Fe2+) interactions.
@en
P2093
P2860
P356
P1476
Structure of the reaction cent ...... inones and Fe2+) interactions.
@en
P2093
P2860
P304
P356
10.1073/PNAS.85.22.8487
P407
P577
1988-11-01T00:00:00Z