Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers
about
Energy transduction: proton transfer through the respiratory complexesStructure of the cytochrome b6f complex: quinone analogue inhibitors as ligands of heme cnThe hepatitis C virus RNA-dependent RNA polymerase membrane insertion sequence is a transmembrane segment.A histidine residue acting as a controlling site for dioxygen reduction and proton pumping by cytochrome c oxidaseEffects of Zinc on Particulate Methane Monooxygenase Activity and StructureIs there a conserved interaction between cardiolipin and the type II bacterial reaction center?Inhibition of rat liver and kidney arginase by cadmium ionTime-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction centerIdentification 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+.Hyperfine and nuclear quadrupole tensors of nitrogen donors in the Q(A) site of bacterial reaction centers: correlation of the histidine N(δ) tensors with hydrogen bond strength.Induced conformational changes upon Cd2+ binding at photosynthetic reaction centersProtein-cofactor interactions in bacterial reaction centers from Rhodobacter sphaeroides R-26: II. Geometry of the hydrogen bonds to the primary quinone formula by 1H and 2H ENDOR spectroscopy.Proton transfer pathways and mechanism in bacterial reaction centers.New tetragonal form of reaction centers from Rhodobacter sphaeroides and the involvement of a manganese ion at a crystal contact point.X-Ray absorption studies of Zn2+ binding sites in bacterial, avian, and bovine cytochrome bc1 complexes.Hydrogen bonding between the Q(B) site ubisemiquinone and Ser-L223 in the bacterial reaction center: a combined spectroscopic and computational perspective.Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase.Ligand identification using electron-density map correlationsRedox potential tuning through differential quinone binding in the photosynthetic reaction center of Rhodobacter sphaeroides.Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry pointThe three-dimensional structures of bacterial reaction centers.Zinc inhibition of bacterial cytochrome bc(1) reveals the role of cytochrome b E295 in proton release at the Q(o) site.Multiple scattering x-ray absorption studies of Zn2+ binding sites in bacterial photosynthetic reaction centers.Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants.Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coliHydrogen bonding and spin density distribution in the Qb semiquinone of bacterial reaction centers and comparison with the Qa site.9-Amino-acridinium bis-(pyridine-2,6-dicarboxyl-ato-κ(3)O(2),N,O(6))ferrate(III) tetra-hydrate.Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides.Zinc ions inhibit oxidation of cytochrome c oxidase by oxygen.Membrane potential-controlled inhibition of cytochrome c oxidase by zinc.Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants.The heme-copper oxidase superfamily shares a Zn2+-binding motif at the entrance to a proton pathway.Characterization of mercury(II)-induced inhibition of photochemistry in the reaction center of photosynthetic bacteria.Zinc ions selectively inhibit steps associated with binding and release of NADP(H) during turnover of proton-translocating transhydrogenase.
P2860
Q22255654-CE402B29-5426-4376-83D6-A625D8950A20Q24681494-68A24D15-0436-46BF-8E1D-39B0424F5466Q27472921-342CFADF-E581-42BC-BABD-0D47269622D3Q27644655-7CC6E6DC-C9EC-45A7-AA3B-4F257FF103E7Q27684382-995A3C06-0E34-4C1B-9690-0E183341CC9EQ28353894-93B0A8E7-6953-43D5-B5DD-B2E34700F378Q28579999-85CC706B-392B-4B6E-9C5C-63CC48AB8EC4Q30830166-AFD3D512-1D6A-4BD7-B4F5-18890DE60BDEQ31514386-DD591B82-55A5-4698-A33F-F6EE05A0640AQ34020565-F258D112-F24D-465A-827B-53E627998489Q34132176-16AA90F4-70ED-4F25-BB4F-5930840E576AQ35545505-AD32FF8F-65FA-4B65-8338-6A26309408AFQ35589966-EA2E28CE-5331-4299-83D0-64AF6FD0819FQ35950758-CFF11F4A-DE87-4F97-B56F-37B16487B1BBQ36008681-75A6628D-46EB-471A-B3EC-A5B934048934Q36595184-D23B7FDB-11DD-40EB-A9D0-7341475CD614Q36663543-96B422FC-7F3F-4891-A75B-F2FF7400E401Q36790447-C0D8B877-4286-4127-A222-A8D254B35D2DQ37047643-7E39120B-35B9-4E47-A57B-94437293C90CQ37282071-D7016B03-7A8A-4037-9E5C-2A972DF45F95Q38098080-3DF9CB92-4A4D-4FE1-8DEA-54A021E32103Q38636646-7C147869-3FB3-4148-8271-66B9A03A7FA6Q40320883-09979730-7532-496B-8231-0EEDB53C4DCFQ41503405-8ACBFF13-3A13-4FCF-80D2-5594FE56DF27Q41646100-37F4D4C1-AF92-4A2F-9392-73B88E4D2D54Q41788791-E9BF2C0A-3F07-4E5F-A59F-72F687731F94Q42140058-31AE1ED5-90CD-41D7-BA5E-52F2FBFA09B0Q42173725-B0F43575-ECDB-4E3E-8CD7-9BDC7A0998FAQ43580824-D7276A4D-EF02-401B-8B34-E4577C2BA967Q43879377-EDE83512-71F6-49C0-B1DE-549031593177Q45214716-A6FB23C2-EDAC-4798-8C1B-0D65BC6E4314Q46959104-256AF717-5F5C-49FB-80DB-9626A1803A6FQ47247186-316F4500-51D5-45FB-A59F-6F9910BA0231Q54486507-5B3F7593-F32A-4454-93D4-111FC7A4FA6C
P2860
Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers
description
2000 nî lūn-bûn
@nan
2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Determination of the binding s ...... in bacterial reaction centers
@ast
Determination of the binding s ...... in bacterial reaction centers
@en
Determination of the binding s ...... in bacterial reaction centers
@nl
type
label
Determination of the binding s ...... in bacterial reaction centers
@ast
Determination of the binding s ...... in bacterial reaction centers
@en
Determination of the binding s ...... in bacterial reaction centers
@nl
prefLabel
Determination of the binding s ...... in bacterial reaction centers
@ast
Determination of the binding s ...... in bacterial reaction centers
@en
Determination of the binding s ...... in bacterial reaction centers
@nl
P2093
P2860
P356
P1476
Determination of the binding s ...... in bacterial reaction centers
@en
P2093
E C Abresch
H L Axelrod
M L Paddock
M Y Okamura
P2860
P304
P356
10.1073/PNAS.97.4.1542
P407
P577
2000-02-15T00:00:00Z