Conformational gating of the electron transfer reaction QA-.QB --> QAQB-. in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay.
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Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centersLeucine 41 is a gate for water entry in the reduction of Clostridium pasteurianum rubredoxinThermochemistry of proton-coupled electron transfer reagents and its implicationsElectron transfer in cyanobacterial photosystem I: II. Determination of forward electron transfer rates of site-directed mutants in a putative electron transfer pathway from A0 through A1 to FX.Identification of the proton pathway in bacterial reaction centers: replacement of Asp-M17 and Asp-L210 with asn reduces the proton transfer rate in the presence of Cd2+.Residual water modulates QA- -to-QB electron transfer in bacterial reaction centers embedded in trehalose amorphous matrices.Induced conformational changes upon Cd2+ binding at photosynthetic reaction centersSelf-regulation phenomena in bacterial reaction centers. I. General theory.Proton coupled electron transfer and redox active tyrosines in Photosystem IIFluorescence relaxation in intact cells of photosynthetic bacteria: donor and acceptor side limitations of reopening of the reaction center.Affinity and activity of non-native quinones at the Q(B) site of bacterial photosynthetic reaction centers.Protein dielectric environment modulates the electron-transfer pathway in photosynthetic reaction centers.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.Aging-associated enzyme human clock-1: substrate-mediated reduction of the diiron center for 5-demethoxyubiquinone hydroxylation.Photosynthetic diode: electron transport rectification by wetting the quinone cofactor.Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+.Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry pointModification of quinone electrochemistry by the proteins in the biological electron transfer chains: examples from photosynthetic reaction centers.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 carbonateA single residue controls electron transfer gating in photosynthetic reaction centers.The nonheme iron in photosystem II.Slow dissociation of a charged ligand: analysis of the primary quinone Q(A) site of photosynthetic bacterial reaction centers.The fe2+ site of photosynthetic reaction centers probed by multiple scattering x-ray absorption fine structure spectroscopy: improving structure resolution in dry matricesCumulant analysis of charge recombination kinetics in bacterial reaction centers reconstituted into lipid vesicles.Photosynthetic electron transfer controlled by protein relaxation: analysis by Langevin stochastic approach.Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: trapping of conformational substates at room temperature.The position of QB in the photosynthetic reaction center depends on pH: a theoretical analysis of the proton uptake upon QB reduction.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.Early bacteriopheophytin reduction in charge separation in reaction centers of Rhodobacter sphaeroides.Electron tunneling through sensitizer wires bound to proteins.Light induced EPR spectra of reaction centers from Rhodobacter sphaeroides at 80K: Evidence for reduction of Q(B) by B-branch electron transfer in native reaction centers.Activation of Electron-Deficient Quinones through Hydrogen-Bond-Donor-Coupled Electron TransferElectron transfer from cytochrome c(2) to the reaction center: a transition state model for ionic strength effects due to neutral mutations.Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site.The DMPC lipid phase transition influences differently the first and the second electron transfer reactions in bacterial reaction centers.George Feher: a pioneer in reaction center research.Temperature and cryoprotectant influence secondary quinone binding position in bacterial reaction centers.Exploring the primary electron acceptor (QA)-site of the bacterial reaction center from Rhodobacter sphaeroides. Binding mode of vitamin K derivatives.Spectrally silent light induced conformation change in photosynthetic reaction centers.
P2860
Q27621441-3A5A2F7D-000D-4D13-86FB-FDE6AD264A77Q27631699-1EFAE39F-AC8A-4C5E-B533-BA8E6F4DD04CQ28744066-BC7C6ED0-6F8A-4809-88A0-5E615AD26E58Q31140976-20A3FCE8-A5E7-4BAC-9789-7B6F14FFD4DFQ31514386-AA71D1B8-3FDB-448A-A3D6-BC31633D7D9DQ33193296-92F21E12-454E-45C7-8584-7BD1A413C230Q34132176-BD8D9D64-47C5-4530-9E3D-2773782BB864Q34173778-C22010BF-344E-4624-951E-AC09D2CDDAC6Q35189808-4BB3BAAD-7C6F-4677-8A41-85F63E34A99EQ35531355-EEB5F59D-6154-490F-885B-0A1BD91570CDQ35642136-C3DA4BE7-2F15-4CDC-A291-7F60F3E1BFA9Q36379167-716F5751-120F-445F-BAC5-DC4B396B5559Q36484728-0BC554A7-D495-4E42-828A-9F14C1BE5C17Q36595184-926D2F2B-2B71-4153-9914-B8FCAB1CB925Q36736063-D5993EB0-D66F-4FAC-9FCC-72E6098D2FD4Q36757281-E69667F8-2A27-4EE4-85F9-F91C85C755AFQ37200776-1484BA26-82D0-445D-A2A6-D0CEBD8FC618Q37282071-120B2BB9-E31D-4A14-8AA1-051B7CD0D539Q37315527-E3F80833-7C85-40DE-B313-18360E54C071Q37373411-7507911A-32CF-4F79-9617-4295B5075C30Q37704750-07AA4E22-6A90-4DE4-95ED-A9A72EFC5E0FQ38146848-56143685-96B6-4D6B-8F39-CA763C47C3DCQ38835907-9A81506B-00F9-44F5-B174-B9CF4392796EQ39594202-4C7894EC-48E2-4462-B2AF-89816CBF6425Q40169445-880EEB72-A117-410B-8BD9-CE4778419E93Q40179275-4A58B4D4-F006-495B-A04C-43B6BC4CA073Q40200299-59854DDB-C7A4-4AD8-BB67-878836C63925Q40232606-8F36A2CB-BEF0-42EA-9528-B78A07DE9247Q41128252-26126A2C-87B3-44C0-9DA5-61AEA6EC3BF8Q41541962-FDF380B6-F929-4A11-A653-A36A7C09FBE0Q41948469-7F9EFCB3-DA96-4383-978A-B180183E70DCQ42162533-38AC4628-26B2-4A6F-A811-8A21DD0EA3A3Q42364294-40875594-0823-4DDC-90C8-6A06C4F0B744Q42959096-ADE86F7F-888C-4CD2-B18C-E5DB39C3EA62Q43647823-F4351960-F8AE-479E-9BB1-123FFC6C8477Q44234581-5D4A9BB2-2610-4159-BDEE-9A19FA316D38Q44387204-02B14CCD-BED4-4211-9A8F-2112B3BECA46Q44976576-2316EB9D-5907-41B5-BEE4-6C5218E38162Q45713863-51718B6D-CB13-46E3-8DFF-EFBB51B489FBQ46327487-7A349343-0C6C-4232-8918-FBE24CCF8D7D
P2860
Conformational gating of the electron transfer reaction QA-.QB --> QAQB-. in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay.
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Conformational gating of the e ...... ined by a driving force assay.
@ast
Conformational gating of the e ...... ined by a driving force assay.
@en
type
label
Conformational gating of the e ...... ined by a driving force assay.
@ast
Conformational gating of the e ...... ined by a driving force assay.
@en
prefLabel
Conformational gating of the e ...... ined by a driving force assay.
@ast
Conformational gating of the e ...... ined by a driving force assay.
@en
P2093
P2860
P356
P1476
Conformational gating of the e ...... ined by a driving force assay.
@en
P2093
P2860
P304
11679-11684
P356
10.1073/PNAS.95.20.11679
P407
P577
1998-09-01T00:00:00Z