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Symmetry matters for the electronic structure of core complexes from Rhodopseudomonas palustris and Rhodobacter sphaeroides PufX-Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose-water amorphous matrices.Light-harvesting complex 1 stabilizes P+QB- charge separation in reaction centers of Rhodobacter sphaeroides.Functional and structural analysis of the photosynthetic apparatus of Rhodobacter veldkampii.Bacterial photosynthetic reaction centers in trehalose glasses: coupling between protein conformational dynamics and electron-transfer kinetics as studied by laser-flash and high-field EPR spectroscopies.Coupling between electron transfer and protein-solvent dynamics: FTIR and laser-flash spectroscopy studies in photosynthetic reaction center films at different hydration levels.Photosynthetic electrogenic events in native membranes ofChloroflexus aurantiacus. Flash-induced charge displacements within the reaction center-cytochromec 554 complex.Retardation of Protein Dynamics by Trehalose in Dehydrated Systems of Photosynthetic Reaction Centers. Insights from Electron Transfer and Thermal Denaturation Kinetics.X-Ray absorption studies of Zn2+ binding sites in bacterial, avian, and bovine cytochrome bc1 complexes.Internal dynamics and protein-matrix coupling in trehalose-coated proteins.Photosynthesis research in Italy: a review.Electron transfer from cytochrome c2 to the primary donor of Rhodobacter sphaeroides reaction centers. A temperature dependence study.Charge recombination kinetics and protein dynamics in wild type and carotenoid-less bacterial reaction centers: studies in trehalose glasses.Zinc inhibition of bacterial cytochrome bc(1) reveals the role of cytochrome b E295 in proton release at the Q(o) site.Protein-matrix coupling/uncoupling in "dry" systems of photosynthetic reaction center embedded in trehalose/sucrose: the origin of trehalose peculiarity.Functionality of photosynthetic reaction centers in polyelectrolyte multilayers: toward an herbicide biosensor.Trehalose preserves the integrity of lyophilized phycoerythrin-antihuman CD8 antibody conjugates and enhances their thermal stability in flow cytometric assays.The fe2+ site of photosynthetic reaction centers probed by multiple scattering x-ray absorption fine structure spectroscopy: improving structure resolution in dry matricesA minimal hypothesis for membrane-linked free-energy transduction. The role of independent, small coupling units.Multiple scattering x-ray absorption studies of Zn2+ binding sites in bacterial photosynthetic reaction centers.Interaction between cytochrome c and the photosynthetic reaction center of purple bacteria: behaviour at low temperature.Mosaic protonic coupling hypothesis for free energy transduction.Cytochrome C in a dry trehalose matrix: structural and dynamical effects probed by x-ray absorption spectroscopy.The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Qo site of bacterial cytochrome bc1.Temperature dependence of charge recombination from the P+QA- and P+QB- states in photosynthetic reaction centers isolated from the thermophilic bacterium Chloroflexus aurantiacus.X-ray absorption studies of Zn(2+)-binding sites in Escherichia coli transhydrogenase and its betaH91K mutant.Kinetics of photosynthetic electron transfer in artificial vesicles reconstituted with purified complexes from Rhodobacter capsulatus. I. The interaction of cytochrome c2 with the reaction center.Electron transfer from HiPIP to the photooxidized tetraheme cytochrome subunit of Allochromatium vinosum reaction center: new insights from site-directed mutagenesis and computational studies.Synergic approach to XAFS analysis for the identification of most probable binding motifs for mononuclear zinc sites in metalloproteins.Electron transfer kinetics in photosynthetic reaction centers embedded in polyvinyl alcohol films.Water Activity Regulates the Q(A)(-) to Q(B) electron transfer in photosynthetic reaction centers from Rhodobacter sphaeroides.EXAFS reveals a structural zinc binding site in the bovine NADH-Q oxidoreductase.Heterogeneity of photosynthetic membranes from Rhodobacter capsulatus: size dispersion and ATP synthase distribution.Local water sensing: water exchange in bacterial photosynthetic reaction centers embedded in a trehalose glass studied using multiresonance EPR.Photochemistry of a photosynthetic reaction center immobilized in lipidic cubic phases.A critical evaluation of the hydropathy profile of membrane proteins.Ionic liquids effects on the permeability of photosynthetic membranes probed by the electrochromic shift of endogenous carotenoids.Protein Immobilization Capabilities of Sucrose and Trehalose Glasses: The Effect of Protein/Sugar Concentration Unraveled by High-Field EPR.Evaluation of the buffer capacity and permeability constant for protons in chromatophores from Rhodobacter capsulatus.Demonstration of a collisional interaction of ubiquinol with the ubiquinol-cytochrome c2 oxidoreductase complex in chromatophores from Rhodobacter sphaeroides.
P50
Q30479462-5B283743-C33C-4DD7-B0FD-848B6DDCAC8CQ31102207-BBF17D03-8380-459A-BDE6-34CEE0CFFF46Q33208547-A0BB89ED-5C18-41A4-8E54-310C3BA24CAEQ33255676-A7B5250B-4F8D-46FC-A5D1-B3F22263B107Q33692029-035905AE-1379-4448-9838-146DC41A45D6Q34053762-1A64CBE9-1ED1-44DF-A138-844904C6988FQ35059804-5179E461-651A-4F51-9C87-F41FED00FB9EQ35666416-D5054379-0A36-4484-87EE-134F31235B84Q36008681-EAD8A6DD-B334-42EC-A9D6-C0149D680C5EQ36123121-443D8494-0B3C-4B9C-A92F-8BBE68EE8CE8Q36498068-8B89440F-4AD9-4C9B-B042-9C64A6C48AE1Q36755827-B999724E-D34B-45A2-B7B9-B072138A5386Q38352422-6332AAD6-00B6-4C84-B509-AD78BE5E0B27Q38636646-B9D13D29-947B-4D0A-A368-8D88BBD7A6ADQ39010280-76D33C62-572C-4001-A8E7-F733E12B482BQ39208461-550AA713-1539-41F0-A728-912C186EC372Q39445441-73DBA7E3-848E-41C7-9D10-3ACB4E990EFAQ39594202-31BB97D9-1065-4F2A-BE0E-998D7149C48CQ40079402-3E7C977A-A6B1-44EC-A103-4CE3E0535314Q40320883-D41686B8-37D1-49C9-84DF-A1B90414AEE0Q40606818-EDB4465A-60F7-4C50-B0DD-3A31D6AFED40Q41558861-A319FB5B-1AB5-478F-8C04-DB8D84615D99Q41964141-BDF36000-6552-4BE8-AC62-57D9D7872026Q42589140-76981B3B-BFE0-4BD0-97B8-9BEA7BAFDBB7Q43017065-5DE8E42B-1B79-4931-A518-D12E05E23727Q43192195-86F66D06-FBC4-41B3-ABFD-4E57B1568481Q43434787-AE78D8EE-0B87-4F0F-97C2-2FD232C1E6D1Q44724462-372AE938-E1E0-416B-A3DC-D51043CD66D4Q44754929-7459C1D1-DA99-49B5-844B-6D29DC78F0C1Q44863007-2CB19521-B574-4D0F-AC0D-5800BA4A46C5Q46521350-4777EBFA-9D80-485E-A835-172FF8C83C8EQ46893980-DF5C217D-C442-46EE-AC15-38A47817B20FQ46931207-42DD6273-13F1-40CB-B9B9-B3EACEB1A99EQ47649363-78EC65BE-8356-44A1-879F-874F6266C3CBQ47865165-AF2D6E29-91AB-4D8B-B152-BD0A0A2A0F94Q50703721-5B9FD403-2E5B-4EE2-AD6A-6CA751F0CE8EQ50858771-DE677329-5EC7-4249-8263-98917AD035A7Q51277345-C5042CFD-3A3D-423C-BA3F-5038754F9D16Q52423789-9D45594A-BCE9-45EE-BD83-C26866610BD8Q52428918-AB5BC614-7E5A-4DA6-9755-E5D527DED3E1
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Giovanni Venturoli
@ast
Giovanni Venturoli
@en
Giovanni Venturoli
@es
Giovanni Venturoli
@nl
Giovanni Venturoli
@sl
type
label
Giovanni Venturoli
@ast
Giovanni Venturoli
@en
Giovanni Venturoli
@es
Giovanni Venturoli
@nl
Giovanni Venturoli
@sl
prefLabel
Giovanni Venturoli
@ast
Giovanni Venturoli
@en
Giovanni Venturoli
@es
Giovanni Venturoli
@nl
Giovanni Venturoli
@sl
P106
P1153
7004036339
P21
P31
P496
0000-0002-9576-1480