{"id":100,"date":"2019-11-24T18:47:14","date_gmt":"2019-11-24T18:47:14","guid":{"rendered":"http:\/\/ebbl.cut.ac.cy\/?page_id=100"},"modified":"2021-02-26T16:15:25","modified_gmt":"2021-02-26T16:15:25","slug":"publications","status":"publish","type":"page","link":"http:\/\/ebbl.cut.ac.cy\/de\/publications\/","title":{"rendered":"(English) Publications"},"content":{"rendered":"\t\t
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Bacterial Colonization on the Surface of Copper Sulfide Minerals Probed by Fourier Transform Infrared Micro-Spectroscopy<\/a><\/p>\n

C Varotsis, M Papageorgiou, C Tselios, KA Yiannakkos, A Adamou, …<\/div>\n
Crystals 10 (11), 1002 , 2020<\/div>\n<\/td>\n
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Photoreduction of carotenoids in the aerobic anoxygenic photoheterotrophs probed by real time Raman spectroscopy<\/a><\/p>\n

M Papageorgiou, C Tselios, C Varotsis<\/div>\n
Journal of Photochemistry and Photobiology B: Biology, 112069 , 2020<\/div>\n<\/td>\n
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Resonance Raman investigation of the Reaction of Cytochrome c Oxidase NO2<\/a><\/p>\n

C Tselios, C Varotsis<\/div>\n
2019-Sustainable Industrial Processing Summit 11, 153-158<\/div>\n<\/td>\n
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Sulfobacillus Thermo Sulfidooxidans Electron Uptake from Cu-Fe Based p Electron Surface-Donors Probed by Raman and FTIR Spectroscopies<\/a><\/p>\n

M Papageorgiou, C Tselios, C Varotsis<\/div>\n
2019-Sustainable Industrial Processing Summit 4, 187-192<\/div>\n<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

Discrete Ligand Binding and Electron Transfer Properties of ba<\/i>3<\/sub>-Cytochrome c<\/i> Oxidase from Thermus thermophilus<\/i>: Evolutionary Adaption to Low Oxygen and \u2026<\/a><\/p>\n

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Bio-hydrometallurgy dynamics of copper sulfide-minerals probed by micro-FTIR mapping and Raman microspectroscopy<\/a><\/p>\n

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Probing hemoglobin glyco-products by fluorescence spectroscopy<\/a><\/p>\n

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Photosensitivity responses of Sagittula stellata probed by FTIR, fluorescence and Raman microspectroscopy<\/a><\/p>\n

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Extracellular electron uptake from carbon-based \u03c0 electron surface-donors: oxidation of graphite sheets by Sulfobacillus thermosulfidooxidans probed by Raman and FTIR \u2026<\/a><\/p>\n

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Reversible temperature-dependent high-to low-spin transition in the heme Fe\u2013Cu binuclear center of cytochrome ba 3 oxidase<\/a><\/p>\n

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Reaction of Hemoglobin With the Schiff Base Intermediate of the Glucose\/Asparagine Reaction: Formation of a Hemichrome<\/a><\/p>\n

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Metal (Ag\/Ti)-containing hydrogenated amorphous carbon nanocomposite films with enhanced nanoscratch resistance: Hybrid PECVD\/PVD system and microstructural characteristics<\/a><\/p>\n

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Modifications of hemoglobin and myoglobin by Maillard reaction products (MRPs)<\/a><\/p>\n

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Detection of Maillard reaction products by a coupled HPLC-Fraction collector technique and FTIR characterization of Cu (II)-complexation with the isolated species<\/a><\/p>\n

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Resonance Raman of ba (3) oxidase from Thermus thermophilus: detection of a ferryl-oxo species and a low to high temperature transition<\/a><\/p>\n

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Nanosecond ligand migration and functional protein relaxation in ba3 oxidoreductase: Structures of the B0, B1 and B2 intermediate states<\/a><\/p>\n

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Probing the whole ore chalcopyrite\u2013bacteria interactions and jarosite biosynthesis by Raman and FTIR microspectroscopies<\/a><\/p>\n

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Identification of the Schiff base intermediate in the Glucose\/Asparagine reaction by coupled HPLC-FTIR spectroscopy<\/a><\/p>\n

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Real time monitoring the Maillard reaction intermediates by HPLC-FTIR<\/a><\/p>\n

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ns-\u03bcs Time-Resolved Step-Scan FTIR of ba3 Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927<\/a><\/p>\n

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Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature<\/a><\/p>\n

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Alleviation of organic solvent inhibition with improved copper recovery from low grade sulphide ore by bioaugmentation with newly isolated Candida sp. OR3 and OR6<\/a><\/p>\n

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Photobiochemical Production of Carbon Monoxide by Thermus<\/i> thermophilus ba<\/i>3<\/sub>\u2010Cytochrome c<\/i> Oxidase<\/a><\/p>\n

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Detection of functional hydrogen-bonded water molecules with protonated\/deprotonated key carboxyl side chains in the respiratory enzyme ba 3-oxidoreductase<\/a><\/p>\n

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Nitric oxide activation by caa 3 oxidoreductase from Thermus thermophilus<\/a><\/p>\n

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Probing the formation of secondary minerals in the bioleaching reactions of chalcopyrite by Raman and FTIR microspectroscopy<\/a><\/p>\n

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Probing the mechanism of acrylamide formation by HPLC-FTIR and Raman spectroscopy<\/a><\/p>\n

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Probing the Action of Cytochrome c<\/i> Oxidase<\/a><\/p>\n

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The protein effect in the structure of two ferryl-oxo intermediates at the same oxidation level in the heme copper binuclear center of cytochrome c oxidase<\/a><\/p>\n

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The structure of two ferryl-oxo intermediates at the same oxidation level in the hemecopper binuclear center of cytochrome c oxidase: the protein effect: SW02. S6\u201331<\/a><\/p>\n

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Detection of the hyponitrite species (HO-N=N-O) in denitrification: Reactivity of NO with the heme Fe-Cu center of cytochrome caa<\/i>3<\/sub> and the heme Fe \u2013Fe center of \u2026<\/a><\/p>\n

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The structure of the hyponitrite in nitric oxide reductase (NOR)<\/a><\/p>\n

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Spectroscopic and Kinetic Investigation of the Fully Reduced and Mixed Valence States of ba3-Cytochrome c Oxidase from Thermus thermophilus A FOURIER TRANSFORM INFRARED (FTIR \u2026<\/a><\/p>\n

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Tuning heme functionality: the cases of Cytochrome c Oxidase and Myoglobin Oxidation<\/a><\/p>\n

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Non-linear vibrational modes in biomolecules: A periodic orbits description<\/a><\/p>\n

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The origin of the FeIV= O intermediates in cytochrome aa3 oxidase<\/a><\/p>\n

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Non-linear vibrational modes in biomolecules: a periodic orbits description<\/a><\/p>\n

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origin of the Fe\u1d35\u2c7d= O intermediates in cytochrome aa\u2083 oxidase<\/a><\/p>\n

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The origin of the Fe IV= O intermediates in cytochrome aa 3 oxidase<\/a><\/p>\n

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Probing protonation\/deprotonation of tyrosine residues in cytochrome ba3 oxidase from Thermus thermophilus by time-resolved step-scan Fourier transform infrared spectroscopy<\/a><\/p>\n

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Regulation of electron and proton transfer by the protein matrix of cytochrome c oxidase<\/a><\/p>\n

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Regulation of electron and proton transfer by the protein matrix of cytochrome C oxidase<\/a><\/p>\n

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Probing protonation\/deprotonation of tyrosine residues in cytochrome ba 3 oxidase from thermus thermophilus by time-resolved step-scan fourier transform infrared spectroscopy<\/a><\/p>\n

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Probing the effect of the proximal and distal to the heme a3 environments in the Cytochrome c Oxidase dioxygen reaction<\/a><\/p>\n

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Vibrational resonances and Cu B displacement controlled by proton motion in cytochrome c oxidase<\/a><\/p>\n

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QM\/MM Calculations on Cyto-chrome c Oxidase: Probing of electron and proton pump coupling<\/a><\/p>\n

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Vibrational resonances and CuB displacement controlled by proton motion in cytochrome c oxidase<\/a><\/p>\n

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Binding and docking interactions of NO, CO and O2 in heme proteins as probed by density functional theory<\/a><\/p>\n

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Heme Cavity Dynamics of Photodissociated CO from ba<\/i>3<\/sub>-Cytochrome c<\/i> Oxidase: The Role of Ring-D Propionate<\/a><\/p>\n

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Binding and docking interactions of NO, CO and O 2 in heme proteins as probed by density functional theory<\/a><\/p>\n

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Cytochrome c Oxidase+ O2 reaction intermediates as probed by Density Functional Theory: The Proximal and Distal to heme a3 effects<\/a><\/p>\n

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Towards the Understanding of His411-FeIV= O Spectroscopic Properties in Ferryl Intermediate of Cytochrome c Oxi-dase+ O2 Reaction: A Theoretical QM\/MM, MD Approach<\/a><\/p>\n

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ORAL PRESENTATION<\/a><\/p>\n

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Assigning vibrational spectra of ferryl-oxo intermediates of cytochrome c oxidase by periodic orbits and molecular dynamics<\/a><\/p>\n

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Nitric oxide activation and reduction by heme\u2013copper oxidoreductases and nitric oxide reductase<\/a><\/p>\n

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Resonance Raman spectroscopy of nitric oxide reductase and cbb 3 heme-copper oxidase<\/a><\/p>\n

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Assigning vibrational spectra of ferryl-oxo intermediates of cytochrome c oxidase by periodic orbits and molecular dynamics<\/a><\/p>\n

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Protein Dynamics and Spectroscopy for Ferryl Intermediate of Cytochrome c<\/i> Oxidase: A Molecular Dynamics Approach<\/a><\/p>\n

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Probing the Environment of CuB<\/sub> in Heme\u2212Copper Oxidases
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The Structure of the Hyponitrite Species in a Heme Fe\uf8ff Cu Binuclear Center<\/a><\/p>\n

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Probing the environment of Cu B in heme-copper oxidases<\/a><\/p>\n

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The structure of the hyponitrite species in a heme Fe-Cu binuclear center<\/a><\/p>\n

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Protein dynamics and spectroscopy for ferryl intermediate of cytochrome c oxidase: a molecular dynamics approach<\/a><\/p>\n

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Two ligand-binding sites in the O2-sensing signal transducer HemAT: Implications for ligand recognition\/discrimination and signaling<\/a><\/p>\n

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Recognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT as revealed by FTIR spectroscopy<\/a><\/p>\n

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Characterization of a bimetallic-bridging intermediate in the reduction of NO to N2O: a density functional theory study<\/a><\/p>\n

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Diogygen activation and bond cleavage in cell respiration as probed by resonance raman spectroscopy<\/a><\/p>\n

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Detection of the His-Heme Fe2+<\/sup>\u2212NO Species in the Reduction of NO to N2<\/sub>O by b<\/i>a<\/i>3<\/sub>-Oxidase from Thermus <\/i>t<\/i>hermophilus<\/i><\/a><\/p>\n

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Structural dynamics of heme\u2013copper oxidases and nitric oxide reductases: time\u2010resolved step\u2010scan Fourier transform infrared and time\u2010resolved resonance Raman studies<\/a><\/p>\n

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Detection of the primary ferrous nitrosyl heme, Fe2+-NO intermediate in the reduction of NO to N20 by cytochrome ba3 oxidase from Thermus thermophilus<\/a><\/p>\n

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Resonance Raman Detection of the Fe2+<\/sup>\u2212C\u2212N Modes in Heme\u2212Copper Oxidases:\u2009 A Probe of the Active Site<\/a><\/p>\n

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Simultaneous Resonance Raman Detection of the Heme a3-Fe-CO and CuB-CO Species in CO-bound ba3-Cytochrome c Oxidase from Thermus thermophilus EVIDENCE FOR A CHARGE TRANSFER CuB \u2026<\/a><\/p>\n

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Detection of a Photostable Five-Coordinate Heme a 3-Fe\u2212 CO Species and Functional Implications of His384\/\u03b110 in CO-Bound ba 3-Cytochrome c Oxidase from Thermus thermophilus<\/a><\/p>\n

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Time-resolved step-scan Fourier transform infrared investigation of heme-copper oxidases: implications for O2 input and H2O\/H+ output channels<\/a><\/p>\n

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Probing the Q-proton pathway of ba3-cytochrome c oxidase by time-resolved Fourier transform infrared spectroscopy<\/a><\/p>\n

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Detection of a Photostable Five-Coordinate Heme a3-Fe-CO Species and Functional Implications of His384\/r10 in CO-Bound ba3-Cytochrome c Oxidase from Thermus thermophilus<\/a><\/p>\n

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ACCELERATED PUBLICATIONS-Simultaneous Resonance Raman Detection of the Heme a3-Fe-CO and CuB-CO Species in CO-bound ba3-Cytochrome c Oxidase from Thermus thermophilus. EVIDENCE \u2026<\/a><\/p>\n

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Detection of a photostable five-coordinate heme a3-Fe-Co species and functional implications of His384\/\u03b110 in CO-bound ba 3-cytochrome c oxidase from Thermus thermophilus<\/a><\/p>\n

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Probing the Q-Proton pathway of ba3-cytochrome c oxidase by time-resolved fourier transform infrared spectroscopy<\/a><\/p>\n

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Time-Resolved Resonance Raman and Time-Resolved Step-Scan FTIR Studies of Nitric Oxide Reductase from Paracoccus denitrificans: Comparison of the Heme b 3-FeB Site to That of \u2026<\/a><\/p>\n

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Ligand binding in a docking site of cytochrome c oxidase: a time-resolved step-scan Fourier transform infrared study<\/a><\/p>\n

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Docking site dynamics of ba3-cytochrome c oxidase from Thermus thermophilus<\/a><\/p>\n

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The Active Site Structure of Heme a 33+ C\u22ee N CuB2+ of Cytochrome aa 3 Oxidase as Revealed from Resonance Raman Scattering<\/a><\/p>\n

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Direct detection of Fe (IV)= O intermediates in the cytochrome aa3 oxidase from Paracoccus denitrificans\/H2O2 reaction<\/a><\/p>\n

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Oxygen-linked Equilibrium CuB-CO Species in Cytochrome ba 3 Oxidase from Thermus thermophilus IMPLICATIONS FOR AN OXYGEN CHANNEL AT THE CuBSITE<\/a><\/p>\n

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Oxygen-linked equilibrium Cu B-CO species in cytochrome ba 3 oxidase from Thermus thermophilus: implications for an oxygen channel at the Cu B site<\/a><\/p>\n

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Docking site dynamics of ba3-cytochrome c oxidase from thermus thermophilus<\/a><\/p>\n

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Ligand binding in a docking site of cytochrome c oxidase: a time-resolved step-scan fourier transform infrared study<\/a><\/p>\n

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ENZYME CATALYSIS AND REGULATION-Direct Detection of Fe (IV)= O Intermediates in the Cytochrome aa3 Oxidase from Paracoccus denitrificans\/H2O2 Reaction.<\/a><\/p>\n

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Oxygen-linked Equilibrium CuB-CO Species in Cytochrome ba3 Oxidase from Thermus thermophilus<\/a><\/p>\n

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Direct Detection of Fe (IV) O Intermediates in the Cytochrome aa<\/a><\/p>\n

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Oxygen-linked Equilibrium Cu<\/a><\/p>\n

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ENZYME CATALYSIS AND REGULATION-Oxygen-linked Equilibrium CuB-CO Species in Cytochrome ba3 Oxidase from Thermus thermophilus. IMPLICATIONS FOR AN OXYGEN CHANNEL AT THE CuB SITE.<\/a><\/p>\n

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Docking Site Dynamics of ba<\/a><\/p>\n

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Fourier transform infrared evidence for a ferric six-coordinate nitrosylheme b 3 complex of cytochrome cbb 3 oxidase from Pseudomonas stutzeri at ambient temperature<\/a><\/p>\n

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Fourier Transform Infrared (FTIR) and Step-scan Time-resolved FTIR Spectroscopies Reveal a Unique Active Site in Cytochromecaa 3 Oxidase from Thermus thermophilus<\/a><\/p>\n

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Observation of the Equilibrium CuB-CO Complex and Functional Implications of the Transient Hemea 3 Propionates in Cytochromeba 3-CO from Thermus thermophilus FOURIER TRANSFORM \u2026<\/a><\/p>\n

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Resonance Raman Detection of a Ferrous Five-Coordinate Nitrosylheme b 3 Complex in Cytochrome cbb 3 Oxidase from Pseudomonas s tutzeri<\/a><\/p>\n

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FTIR and step-scan time-resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 oxidase from Thermus Thermophilus<\/a><\/p>\n

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Nitric-oxide reductase structure and properties of the catalytic site from resonance Raman scattering<\/a><\/p>\n

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The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase<\/a><\/p>\n

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Decay of the Transient CuB<\/sub>\u2212CO Complex Is Accompanied by Formation of the Heme Fe\u2212CO Complex of Cytochrome cbb<\/i>3<\/sub>\u2212CO at Ambient Temperature \u2026<\/a><\/p>\n

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DFT Study of endoperoxides and their in-termediates in Fe (II) cleavage of the endoperoxy bridge<\/a><\/p>\n

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Antimalarial endoperoxides: synthesis and implications of the mode of action<\/a><\/p>\n

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Observation of the equilibrium Cu B-CO complex and functional implications of the transient heme a 3 propionates in cytochrome ba 3-CO from Thermus thermophilus. Fourier \u2026<\/a><\/p>\n

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Nitric-oxide Reductase<\/a><\/p>\n

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ENZYME CATALYSIS AND REGULATION-Observation of the Equilibrium CuB-CO Complex and Functional Implications of the Transient Heme a3 Propionates in Cytochrome ba3-CO from Thermus \u2026<\/a><\/p>\n

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ENZYME CATALYSIS AND REGULATION-Fourier Transform Infrared (FTIR) and Step-scan Time-resolved FTIR Spectroscopies Reveal a Unique Active Site in Cytochrome caa3 Oxidase from \u2026<\/a><\/p>\n

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Observation of the Equilibrium Cu<\/a><\/p>\n

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Antimalarial endoperoxides: synthesis and implications of the mode of action<\/a><\/p>\n

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Fourier transform infrared investigation of non-heme Fe (III) and Fe (II) decomposition of artemisinin and of a simplified trioxane alcohol<\/a><\/p>\n

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Ferryl\u2013oxo heme intermediate in the antimalarial mode of action of artemisinin<\/a><\/p>\n

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Picosecond resonance Raman evidence of the structure of a long-lived electronic excited state of low-spin Fe (III) heme o<\/a><\/p>\n

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Resonance Raman and Fourier Transform Infrared Detection of Azide Binding to the Binuclear Center of Cytochrome bo 3 Oxidase from Escherichia c oli<\/a><\/p>\n

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Infrared observation of CuBCO and deprotonation of a carboxylic side chain for photodissociated CO-cytochrome c oxidase<\/a><\/p>\n

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Fourier transform infrared and resonance Raman studies of the interaction of azide with cytochrome c oxidase from Paracoccus denitrificans<\/a><\/p>\n

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Infrared evidence for CuB ligation of photodissociated CO of cytochrome c oxidase at ambient temperatures and accompanied deprotonation of a carboxyl side chain of protein<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resonance Raman and fourier transform infrared detection of azide binding to the binuclear center of cytochrome bo3, oxidase from Escherichia coli<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

BIOPHYSICAL CHEMISTRY-Fourier Transform Infrared and Resonance Raman Studies of the Interaction of Azide with Cytochrome c Oxidase from Paracoccus denitrificans<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resonance Raman scattering from heme o complexes and cytochrome bo 3 oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resonance Raman Scattering from Heme O Complexes and Cytochrome bo3 0xidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resonance Raman and FTIR Studies of Carbon Monoxide-Bound Cytochrome aa<\/i>3<\/sub>-600 Oxidase of Bacillus subtilis<\/i><\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resonance raman and FTIR studies of carbon monoxide-bound cytochrome aa3-600 oxidase of bacillus subtilis<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Ligand Dynamics in the Binuclear Site in Cytochrome Oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Low-power picosecond resonance Raman evidence for histidine ligation to heme a 3 after photodissociation of CO from cytochrome c oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Dioxygen activation in enzymatic systems and in inorganic models<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Cytochrome o3 hemepocket relaxation subsequent to carbon monoxide photolysis from fully reduced and mixed valence cytochrome bo3 oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Cytochrome o<\/i>3<\/sub> hemepocket relaxation subsequent to carbon monoxide photolysis from fully reduced and mixed valence cytochrome bo<\/i>3<\/sub> oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resonance Raman spectroscopy of the heme groups of cytochrome cbb3 in Rhodobacter sphaeroides<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Photolytic activity of early intermediates in dioxygen activation and reduction by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resonance raman spectroscopy of the heme groups of cytochrome cbb3 in hodobacter sphaeroides<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Photolytic activity of early intermediates in dioxygen activation and reduction by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Raman detection of a peroxy intermediate in the hydroquinone-oxidizing cytochrome aa3, of Bacillus subtilis<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Nickel Coordination Chemistry with Oxothiolate Ligands and Its Relevance to Hydrogenase Enzymes<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Photodissociated Cytochrome bo Oxidase: A Time-Resolved Raman Study of the FE-HIS Stretching Mode<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Syntheses, structures, and properties of six novel alkali metal tin sulfides: K2Sn2S8,. alpha.-Rb2Sn2S8,. beta.-Rb2Sn2S8, K2Sn2S5, Cs2Sn2S6, and Cs2SnS14<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Syntheses, structures, and properties of six novel alkali metal tin sulfides: K2Sn2S8, \u03b1-Rb2Sn2S8, \u03b2-Rb2Sn2S8, K2Sn2S5, Cs2Sn2S6, and Cs2SnS14<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resolution of the reaction sequence during the reduction of O2 by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Dioxygen activation and reduction by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Dioxygen Reduction by Cytochrome Oxidase: A Proton-Transfer Limited Reaction<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

[17] Nanosecond time-resolved resonance Raman spectroscopy<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Resolution of the reaction sequence during the reduction of O2 by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Optical and resonance Raman spectroscopy of the heme groups of the quinol-oxidizing cytochrome aa3 of Bacillus subtilis<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

O2 activation in cytochrome oxidase and in other heme proteins<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

STRUCTURE, SYNTHESIS, AND DIOXYGEN BINDING OF THE HEME OMICRON PROSTHETIC GROUP FROM THE TERMINAL QUINOL OXIDASE OF ESCHERICHIA-COLI<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Structure of the heme o prosthetic group from the terminal quinol oxidase of Escherichia coli<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Optical and Resonance Raman Spectroscopy of the Heme Groups of the Quinol-Oxidizing Cytochrome a43 of Bacillus subtilist<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

DETECTION AND PHOTOLYSIS OF TRANSIENT SPECIES IN THE CYTOCHROME-OXIDASE O2 REACTION<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

RESONANCE RAMAN-SPECTROSCOPY OF CYTOCHROME-OO3 AND MODEL COMPOUNDS<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Time-resolved resonance Raman detection of intermediates in the reduction of dioxygen by cytochrome oxidase.<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Appearance of the. nu.(FeIV: O) vibration from a ferryl-oxo intermediate in the cytochrome oxidase\/dioxygen reaction<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Direct detection of a dioxygen adduct of cytochrome a3 in the mixed valence cytochrome oxidase\/dioxygen reaction.<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

A simple mixer\/jet cell for raman spectroscopic studies<\/a><\/p>\n

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\n

A simple mixer\/jet cell for raman spectroscopic studies<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Time-resolved Raman detection of. mu.(Fe-O) in an early intermediate in the reduction of oxygen by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Appearance of the \u03bd (Feiv= O) vibration from a ferry1-oxo intermediate in the cytochrome oxidase\/dioxygen reaction<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Direct detection of a dioxygen adduct of cytochrome a3 in the mixed valence cytochrome oxidase\/dioxygen reaction<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Time-resolved resonance Raman detection of intermediates in the reduction of dioxygen by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Time-resolved Raman detection of. mu.(Fe-O) in an early intermediate in the reduction of oxygen by cytochrome oxidase [Erratum to document cited in CA111 (9): 73737r]<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Time-resolved Raman detection of. nu.(Fe-O) in an early intermediate in the reduction of oxygen by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

RAMAN-SPECTROSCOPY OF INTERMEDIATES IN HEME PROTEIN CATALYSIS<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

Time-resolved raman detection of v (Fe-O) in an early intermediate in the reduction of O2 by cytochrome oxidase<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

RESONANCE RAMAN-SCATTERING FROM INTERMEDIATES IN HEME PROTEIN CATALYSIS<\/a><\/p>\n

 <\/td>\n <\/td>\n<\/tr>\n
\n

A resonance Raman study of the higher-lying electronic states of styrene vapor<\/a><\/p>\n

LD Ziegler, C Varotsis<\/div>\n
Chemical physics letters 123 (3), 175-18<\/div>\n<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<\/div>\n<\/div>\n<\/div>\n<\/div>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t<\/div>\n\t\t","protected":false},"excerpt":{"rendered":"

Publications Bacterial Colonization on the Surface of Copper Sulfide Minerals Probed by Fourier Transform Infrared Micro-Spectroscopy C Varotsis, M Papageorgiou, C Tselios, KA Yiannakkos, A Adamou, … Crystals 10 (11), 1002 , 2020     Photoreduction of carotenoids in the … Weiter<\/a><\/p>\n","protected":false},"author":55,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-100","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/pages\/100","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/users\/55"}],"replies":[{"embeddable":true,"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/comments?post=100"}],"version-history":[{"count":20,"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/pages\/100\/revisions"}],"predecessor-version":[{"id":252,"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/pages\/100\/revisions\/252"}],"wp:attachment":[{"href":"http:\/\/ebbl.cut.ac.cy\/de\/wp-json\/wp\/v2\/media?parent=100"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}