The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB
about
Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transferA fresh look at the evolution and diversification of photochemical reaction centersStructure of fumarate reductase from Wolinella succinogenes at 2.2 A resolutionStructural details of an interaction between cardiolipin and an integral membrane proteinStructural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolutionA third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reductionInteractions between lipids and bacterial reaction centers determined by protein crystallographyIs there a conserved interaction between cardiolipin and the type II bacterial reaction center?Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction centerConformationally controlled pK-switching in membrane proteins: one more mechanism specific to the enzyme catalysis?Pathways for proton release during ubihydroquinone oxidation by the bc(1) complex.Key role of proline L209 in connecting the distant quinone pockets in the reaction center of Rhodobacter sphaeroides.Steered molecular dynamics simulation of the Rieske subunit motion in the cytochrome bc(1) complex.Insights from the structure of the yeast cytochrome bc1 complex: crystallization of membrane proteins with antibody fragments.Succinate:quinone oxidoreductases--what can we learn from Wolinella succinogenes quinol:fumarate reductase?Stigmatellin probes the electrostatic potential in the QB site of the photosynthetic reaction center.The role of electrostatics in proton-conducting membrane protein complexes.Observations concerning the quinol oxidation site of the cytochrome bc1 complex.Characterization of the quinones in purple sulfur bacterium Thermochromatium tepidum.Conformational relaxation and water penetration coupled to ionization of internal groups in proteins.Hydrogen-bonded networks along and bifurcation of the E-pathway in quinol:fumarate reductase.Trapped conformational states of semiquinone (D+*QB-*) formed by B-branch electron transfer at low temperature in Rhodobacter sphaeroides reaction centersHydrogen bonding between the Q(B) site ubisemiquinone and Ser-L223 in the bacterial reaction center: a combined spectroscopic and computational perspective.Proton translocation by the cytochrome bc1 complexes of phototrophic bacteria: introducing the activated Q-cycle.Proton uptake by bacterial reaction centers: the protein complex responds in a similar manner to the reduction of either quinone acceptorEssential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductaseMetalloproteins containing cytochrome, iron-sulfur, or copper redox centersStructure of the H subunit of the photosynthetic reaction center from the thermophilic purple sulfur bacterium, Thermochromatium tepidum Implications for the specific binding of the lipid molecule to the membrane protein complex.Slow dissociation of a charged ligand: analysis of the primary quinone Q(A) site of photosynthetic bacterial reaction centers.Evaluation of a biohybrid photoelectrochemical cell employing the purple bacterial reaction centre as a biosensor for herbicides.Natural resistance to inhibitors of the ubiquinol cytochrome c oxidoreductase of Rubrivivax gelatinosus: sequence and functional analysis of the cytochrome bc(1) complex.Kinetics, energetics, and electronic coupling of the primary electron transfer reactions in mutated reaction centers of Blastochloris viridis.The position of QB in the photosynthetic reaction center depends on pH: a theoretical analysis of the proton uptake upon QB reduction.Dynamic water networks in cytochrome C oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations.Crystallographic refinement of ligand complexes.ENDOR spectroscopy reveals light induced movement of the H-bond from Ser-L223 upon forming the semiquinone (Q(B)(-)(*)) in reaction centers from Rhodobacter sphaeroides.Molecular dynamics simulation of water in cytochrome c oxidase reveals two water exit pathways and the mechanism of transport.Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site.Three molecules of ubiquinone bind specifically to mitochondrial cytochrome bc1 complex.
P2860
Q24535858-CE7E580B-3BE1-4B01-8988-8E11D1CC32E0Q24669818-3F82FD27-F654-4853-8800-7F8A9427EA14Q27002689-D0044843-793A-4610-8B2B-06EA57A3AF96Q27620575-F66B76B1-B49A-40AC-9C48-74B589651A1AQ27620814-5E585F71-78A5-42F1-9F9A-C3D78DFD94F1Q27627217-648BECB5-1D45-4110-B8A5-058C2A52C4A0Q27630634-44963013-C544-4FA3-BC66-80B68FBD4F87Q27639471-D06C317D-AA69-4329-8F8D-25D80BAC3430Q28353894-BFDFC9CC-01AC-4D55-AA3F-136D0C367505Q30830166-60CABEE8-72B7-4488-A3D6-BC72078AC612Q33801133-E2CBDB40-6DDF-4CD7-9EBA-979F2DE50587Q33872609-B42A9273-C7A3-41F9-9C1E-C1C38DCF112EQ34067300-9D204B72-C8A5-4CD1-A83D-0B1FC8C42251Q34171405-575A01EE-4FCE-451A-BCEE-30FD2A422B45Q34353253-30A0295B-CD6F-4ACB-9026-6363137F98EDQ34353261-171320CE-3BD3-4D86-B0A8-470F86465185Q34996640-109A581E-F5EA-41ED-9BDD-CD014EC5E130Q35146229-9F2B22D4-A580-4CD7-8964-960D250FEB11Q35589952-8F89F1C3-0B8E-4705-AC90-83C600A898FFQ35655166-B51DFBA0-8159-4B5D-914F-30E53AC43179Q36027195-CEACE5D1-D15E-4064-AF0F-BDAA0CBD796BQ36246558-5CA11315-8EDB-405F-90D2-997E35292CD1Q36484728-1978550E-F3D7-4ACD-9B40-330D62FE746FQ36595184-C2CF1627-B604-4564-865B-3A90842C2776Q36698146-29B4B7B1-9B8D-4362-BE93-90FC8DBCE326Q36744804-6A109D84-B3FA-4D72-A665-D58B6E148B4BQ37280285-9D8FF1A3-6538-4BDF-948D-F426A42B677EQ37727718-21201D00-9683-42A5-BF90-B3379772652CQ38301478-500588FB-21A6-4B5F-BC00-C7B148BDDC31Q38835907-EDEDEA55-C66A-4E2B-925D-999A389274F3Q39202208-F5370CFF-E7C9-4933-B48A-6C11CE99A613Q39679684-0DD5341E-7EC2-45D1-ADCC-EC7D45D4236BQ40208639-F89A046C-FD51-4459-80D3-91D7345B9510Q40232606-96B67D2D-E71B-438B-AD34-ED60DED131CAQ40276973-36BAAE28-FAAC-4FA1-9F81-E54A8264DA1DQ40886998-17519190-9032-4845-B2E2-E008FA3C14ACQ41128252-81661C3D-A3CF-4D3A-AC8B-91EDB4173116Q42975917-64490CAD-F5C8-47C8-829B-9EF7F0C4AC61Q43647823-5ABC34FC-ECBD-4AF5-9701-A48E3DF3FF40Q43693164-6F66962B-3F2F-4E5F-8373-F3BF85271ECE
P2860
The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB
description
1997 nî lūn-bûn
@nan
1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
The coupling of light-induced ...... e of the secondary quinone, QB
@ast
The coupling of light-induced ...... e of the secondary quinone, QB
@en
The coupling of light-induced ...... e of the secondary quinone, QB
@nl
type
label
The coupling of light-induced ...... e of the secondary quinone, QB
@ast
The coupling of light-induced ...... e of the secondary quinone, QB
@en
The coupling of light-induced ...... e of the secondary quinone, QB
@nl
prefLabel
The coupling of light-induced ...... e of the secondary quinone, QB
@ast
The coupling of light-induced ...... e of the secondary quinone, QB
@en
The coupling of light-induced ...... e of the secondary quinone, QB
@nl
P1433
P1476
The coupling of light-induced ...... e of the secondary quinone, QB
@en
P2093
C R Lancaster
P304
P356
10.1016/S0969-2126(97)00285-2
P577
1997-10-15T00:00:00Z