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Electrochemically Induced Far-Infrared Difference Spectroscopy on Metalloproteins Using Advanced Synchrotron Technology
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Handbook of Vibrational Spectroscopy
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Vibrational Spectroscopy in Life Science
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Profiling the Active Site of a Copper Enzyme through Its Far‐Infrared Fingerprint
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Electrochemically induced FTIR difference spectroscopy in the mid‐ to far infrared (200 μm) domain: A new setup for the analysis of metal–ligand interactions in redox proteins
inferredcites →https://doi.org/10.1002/bip.360250307openalex-snapshot
Examination of the secondary structure of proteins by deconvolved FTIR spectra
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Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands
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Applications of Terahertz Spectroscopy in Biosystems
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Probing the Hydrogen Bonding Structure in the Rieske Protein
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A Combined Far‐Infrared Spectroscopic and Electrochemical Approach for the Study of Iron–Sulfur Proteins
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Bioinorganic Chemistry of Copper
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Solvent-based deuterium isotope effects on the redox thermodynamics of cytochrome c
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Nickel(II)-substituted azurin I from Alcaligenes xylosoxidans as characterized by resonance Raman spectroscopy at cryogenic temperature
inferredcites →https://doi.org/10.1007/s11120-009-9439-xopenalex-snapshot
Fourier transform infrared (FTIR) spectroscopy
inferredcites →https://doi.org/10.1016/0005-2728(90)90206-jopenalex-snapshot
Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli
inferredcites →https://doi.org/10.1016/0014-5793(89)80285-6openalex-snapshot
Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli
inferredcites →https://doi.org/10.1016/0014-5793(96)00076-2openalex-snapshot
The role of His117 in the redox reactions of azurin from Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1016/0022-2836(78)90375-3openalex-snapshot
A crystallographic model for azurin at 3 Å resolution
inferredcites →https://doi.org/10.1016/0022-2836(91)80173-ropenalex-snapshot
Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5·5 and pH 9·0
inferredcites →https://doi.org/10.1016/0022-2860(94)08471-sopenalex-snapshot
Temperature dependence of the optical constants for liquid H2O and D2O in the far IR region
inferredcites →https://doi.org/10.1016/0167-4838(86)90048-8openalex-snapshot
The pH and redox-state dependence of the copper site in azurin from Pseudomonas aeruginosa as studied by EXAFS
inferredcites →https://doi.org/10.1016/b978-0-12-042510-5.x5000-8openalex-snapshot
Fourier Transform Spectrometry
inferredcites →https://doi.org/10.1016/j.bbabio.2007.06.004openalex-snapshot
Infrared spectroscopy of proteins
inferredcites →https://doi.org/10.1016/j.bbapap.2005.03.008openalex-snapshot
Temperature excursion infrared (TEIR) spectroscopy used to study hydrogen bonding between water and biomolecules
inferredcites →https://doi.org/10.1016/j.biotechadv.2012.02.012openalex-snapshot
Biological applications of synchrotron radiation infrared spectromicroscopy
inferredcites →https://doi.org/10.1016/j.chemphys.2005.04.033openalex-snapshot
Far-infrared spectra of amino acids
inferredcites →https://doi.org/10.1016/j.infrared.2006.01.015openalex-snapshot
The AILES Infrared Beamline on the third generation Synchrotron Radiation Facility SOLEIL
inferredcites →https://doi.org/10.1016/j.saa.2010.08.071openalex-snapshot
Intermolecular vibrational study in liquid water and ice by using far infrared spectroscopy with synchrotron radiation of MIRRORCLE 20
inferredcites →https://doi.org/10.1016/j.tibtech.2006.11.002openalex-snapshot
Adding synchrotron radiation to infrared microspectroscopy: what's new in biomedical applications?
inferredcites →https://doi.org/10.1016/s0006-3495(03)74562-7openalex-snapshot
Protein Flexibility and Conformational State: A Comparison of Collective Vibrational Modes of Wild-Type and D96N Bacteriorhodopsin
inferredcites →https://doi.org/10.1021/ac300308xopenalex-snapshot
Synchrotron Infrared Measurements of Protein Phosphorylation in Living Single PC12 Cells during Neuronal Differentiation
inferredcites →https://doi.org/10.1021/bc900270aopenalex-snapshot
Protein Binding and the Electronic Properties of Iron(II) Complexes: An Electrochemical and Optical Investigation of Outer Sphere Effects
inferredcites →https://doi.org/10.1021/bi00157a006openalex-snapshot
Complete sequential proton and nitrogen-15 nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1021/bi001751gopenalex-snapshot
Identification of a Mn−O−Mn Cluster Vibrational Mode of the Oxygen-Evolving Complex in Photosystem II by Low-Frequency FTIR Spectroscopy
inferredcites →https://doi.org/10.1021/bi0022994openalex-snapshot
D1-Asp170 Is Structurally Coupled to the Oxygen Evolving Complex in Photosystem II As Revealed by Light-Induced Fourier Transform Infrared Difference Spectroscopy
inferredcites →https://doi.org/10.1021/bi00301a008openalex-snapshot
Resonance Raman spectra of blue copper proteins: assignments from normal mode calculations and copper-63/copper-65 and H2O/D2O shifts for stellacyanin and laccase
inferredcites →https://doi.org/10.1021/bi035420qopenalex-snapshot
Changes of Low-Frequency Vibrational Modes Induced by Universal15N- and13C-Isotope Labeling in S2/S1FTIR Difference Spectrum of Oxygen-Evolving Complex
inferredcites →https://doi.org/10.1021/bi0362323openalex-snapshot
Mid- to Low-Frequency Fourier Transform Infrared Spectra of S-State Cycle for Photosynthetic Water Oxidation inSynechocystissp. PCC 6803
inferredcites →https://doi.org/10.1021/bi3006434openalex-snapshot
Temperature Dependence of Water Interactions with the Amide Carbonyls of α-Helices
inferredcites →https://doi.org/10.1021/ic050553gopenalex-snapshot
A Detailed Resonance Raman Spectrum of Nickel(II)-Substituted Pseudomonas aeruginosa Azurin
inferredcites →https://doi.org/10.1021/ic060450dopenalex-snapshot
Spectroscopic Methods in Bioinorganic Chemistry: Blue to Green to Red Copper Sites
inferredcites →https://doi.org/10.1021/ic900145nopenalex-snapshot
Cadmium(II) Cysteine Complexes in the Solid State: A Multispectroscopic Study
inferredcites →https://doi.org/10.1021/j100277a034openalex-snapshot
Specific hydrogen-bonding contributions to the thermodynamics and kinetics of electron transfer. Modifications to the classical and semiclassical theories of electron transfer
inferredcites →https://doi.org/10.1021/ja00306a025openalex-snapshot
Resonance Raman studies of blue copper proteins: effects of temperature and isotopic substitutions. Structural and thermodynamic implications
inferredcites →https://doi.org/10.1021/jp064690qopenalex-snapshot
Water Effects on Electron Transfer in Azurin Dimers
inferredcites →https://doi.org/10.1021/jp068773iopenalex-snapshot
Water-Mediated Electron Transfer between Protein Redox Centers
inferredcites →https://doi.org/10.1021/jp810774gopenalex-snapshot
Low-Frequency Heme, Iron-Ligand, and Ligand Modes of Imidazole and Imidazolate Complexes of Iron Protoporphyrin and Microperoxidase in Aqueous Solution. An Analysis by Far-Infrared Difference Spectroscopy
inferredcites →https://doi.org/10.1038/nmeth.1585openalex-snapshot
High-resolution Fourier-transform infrared chemical imaging with multiple synchrotron beams
inferredcites →https://doi.org/10.1038/nsb736openalex-snapshot
Dramatic modulation of electron transfer in protein complexes by crosslinking
inferredcites →https://doi.org/10.1039/b804734kopenalex-snapshot
The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin
inferredcites →https://doi.org/10.1039/b915810copenalex-snapshot
Measurement of metabolite formation in single living cells of Chlamydomonas reinhardtii using synchrotron Fourier-Transform Infrared spectromicroscopy
inferredcites →https://doi.org/10.1063/1.1894929openalex-snapshot
Signatures of the hydrogen bonding in the infrared bands of water
inferredcites →https://doi.org/10.1063/1.3326344openalex-snapshot
Temperature Dependence of the Far Infrared Signature of Internal Hydrogen Bonds in Proteins as Probed for Integrins
inferredcites →https://doi.org/10.1063/1.3686886openalex-snapshot
Far-infrared spectroscopy on free-standing protein films under defined temperature and hydration control
inferredcites →https://doi.org/10.1073/pnas.81.4.1263openalex-snapshot
Temperature dependence of the resonance Raman spectra of plastocyanin and azurin between cryogenic and ambient conditions.
inferredcites →https://doi.org/10.1073/pnas.90.12.5443openalex-snapshot
Electron self-exchange in azurin: calculation of the superexchange electron tunneling rate.
inferredcites →https://doi.org/10.1074/jbc.m505887200openalex-snapshot
Changes in Structural and Functional Properties of Oxygen-evolving Complex Induced by Replacement of D1-Glutamate 189 with Glutamine in Photosystem II
inferredcites →https://doi.org/10.1088/0031-9155/46/9/201openalex-snapshot
The interaction between Terahertz radiation and biological tissue
inferredcites →https://doi.org/10.1107/s0909049509046056openalex-snapshot
Facing the challenge of biosample imaging by FTIR with a synchrotron radiation source
inferredcites →https://doi.org/10.1109/icimw.2010.5613037openalex-snapshot
The AILES beamline for THz and IR spectroscopy
inferredcites →https://doi.org/10.1111/j.1432-1033.1989.tb14540.xopenalex-snapshot
The azurin gene from Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1111/j.1432-1033.1990.tb15338.xopenalex-snapshot
Redox‐linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry
inferredcites →https://doi.org/10.1111/j.1432-1033.1993.tb17661.xopenalex-snapshot
Reduction potentials and their pH dependence in site‐directed‐mutant forms of azurin from Pseudomonas aeruginosa
inferredcites →https://doi.org/10.2116/analsci.24.185openalex-snapshot
Analytical Terahertz Spectroscopy
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1016/b978-0-12-409547-2.11537-9openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-323-85669-0.00092-1openalex-snapshot
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New experimental set-ups for studying nanoconfined water on the AILES beamline at SOLEIL
inferred← citeshttps://doi.org/10.1021/acs.chemrev.9b00449openalex-snapshot
Infrared Difference Spectroscopy of Proteins: From Bands to Bonds
inferred← citeshttps://doi.org/10.1021/acsanm.8b01240openalex-snapshot
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inferred← citeshttps://doi.org/10.1039/c7cc03496bopenalex-snapshot
Far infrared spectroscopy of hydrogen bonding collective motions in complex molecular systems
inferred← citeshttps://doi.org/10.1073/pnas.2108568118openalex-snapshot
Stripping away ion hydration shells in electrical double-layer formation: Water networks matter
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Crystal structure and redox properties of a novel cyanobacterial heme protein with a His/Cys heme axial ligation and a Per-Arnt-Sim (PAS)-like domain
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Stripping off of the Hydration Shells in the Double Layer Formation: Water Networks Matter
inferred← citeshttps://doi.org/10.70675/bf44dc68z5284z40f0zaabezdc5c9847a604openalex-snapshot
Structure and connectivity of water molecules at the interfaces of nanoconfined systems
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