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In Situ Infrared Spectroscopy for the Analysis of Gas-processing Metalloenzymes
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Steric Control of the Hi‐CO MoFe Nitrogenase Complex Revealed by Stopped‐Flow Infrared Spectroscopy
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Infrared Spectroscopy During Electrocatalytic Turnover Reveals the Ni‐L Active Site State During H2 Oxidation by a NiFe Hydrogenase
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[FeFe]‐Hydrogenase with Chalcogenide Substitutions at the H‐Cluster Maintains Full H2 Evolution Activity
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Proton‐Coupled Reduction of the Catalytic [4Fe‐4S] Cluster in [FeFe]‐Hydrogenases
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A [RuRu] Analogue of an [FeFe]‐Hydrogenase Traps the Key Hydride Intermediate of the Catalytic Cycle
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Cysteine SH and Glutamate COOH Contributions to [NiFe] Hydrogenase Proton Transfer Revealed by Highly Sensitive FTIR Spectroscopy
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CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution
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Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site
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Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes
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The Molecular Mechanism of Membrane Proteins Probed by Evanescent Infrared Waves
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Synergic Binding of Carbon Monoxide and Cyanide to the FeMo Cofactor of Nitrogenase: Relic Chemistry of an Ancient Enzyme?
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Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein
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Sunlight‐Dependent Hydrogen Production by Photosensitizer/Hydrogenase Systems
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Photolysis of Hi‐CO Nitrogenase – Observation of a Plethora of Distinct CO Species Using Infrared Spectroscopy
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Sodium and Potassium Ions in Proteins and Enzyme Catalysis
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Infrared Membrane Spectroscopy
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Hydrogen production by Chlamydomonas reinhardtii: an elaborate interplay of electron sources and sinks
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The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy
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The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase
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Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy
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Determination of the unfrozen water content of maximally freeze-concentrated carbohydrate solutions
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Attenuated total reflection
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Infrared spectroscopy of proteins
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Structure and function of bacterial nitric oxide reductases
inferredcites →https://doi.org/10.1016/j.bbabio.2014.07.007openalex-snapshot
FTIR studies of metal ligands, networks of hydrogen bonds, and water molecules near the active site Mn4CaO5 cluster in Photosystem II
inferredcites →https://doi.org/10.1016/j.bbabio.2014.08.002openalex-snapshot
Infrared and Raman spectroscopic investigation of the reaction mechanism of cytochrome c oxidase
inferredcites →https://doi.org/10.1016/j.bbabio.2018.05.018openalex-snapshot
Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy
inferredcites →https://doi.org/10.1016/j.bbamem.2013.04.026openalex-snapshot
Surface-enhanced infrared absorption spectroscopy (SEIRAS) to probe monolayers of membrane proteins
inferredcites →https://doi.org/10.1016/j.bbapap.2013.07.015openalex-snapshot
Recent applications of ATR FTIR spectroscopy and imaging to proteins
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Operando methodology: combination of in situ spectroscopy and simultaneous activity measurements under catalytic reaction conditions
inferredcites →https://doi.org/10.1016/j.cbpa.2014.11.019openalex-snapshot
Light-driven hydrogen production from Photosystem I-catalyst hybrids
inferredcites →https://doi.org/10.1016/j.febslet.2013.06.055openalex-snapshot
The [NiFe]‐hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron‐ and carbon dioxide‐binding proteins
inferredcites →https://doi.org/10.1016/j.ymeth.2018.02.012openalex-snapshot
Methods of reconstitution to investigate membrane protein function
inferredcites →https://doi.org/10.1016/s0006-3495(02)75368-xopenalex-snapshot
Transient Binding of CO to CuB in Cytochrome c Oxidase Is Dynamically Linked to Structural Changes around a Carboxyl Group: A Time-Resolved Step-Scan Fourier Transform Infrared Investigation
inferredcites →https://doi.org/10.1016/s0014-5793(96)01174-xopenalex-snapshot
Redox FTIR difference spectroscopy using caged electrons reveals contributions of carboxyl groups to the catalytic mechanism of haemcopper oxidases
inferredcites →https://doi.org/10.1016/s0021-9258(19)39023-4openalex-snapshot
Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase. Implications regarding oxygen reduction.
inferredcites →https://doi.org/10.1016/s0021-9258(19)68085-3openalex-snapshot
Dynamic interactions of CO with a3Fe and CuB in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures.
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The Theory of Pressure Effects on Enzymes
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[12] Fourier transform infrared photolysis studies of caged compounds
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Photo-lability of CO bound to Mo-nitrogenase from Azotobacter vinelandii
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Proton Transfer Mechanisms in Bimetallic Hydrogenases
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Applications of Photogating and Time Resolved Spectroscopy to Mechanistic Studies of Hydrogenases
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Structural Enzymology of Nitrogenase Enzymes
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Surface-Enhanced Infrared Spectroscopy Using Resonant Nanoantennas
inferredcites →https://doi.org/10.1021/acs.chemrev.7b00664openalex-snapshot
Oxygen Activation and Energy Conservation by Cytochrome c Oxidase
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Infrared Difference Spectroscopy of Proteins: From Bands to Bonds
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The Spectroscopy of Nitrogenases
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Reactivity, Mechanism, and Assembly of the Alternative Nitrogenases
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Temperature Dependence of Structural Dynamics at the Catalytic Cofactor of [FeFe]-hydrogenase
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The Laser-Induced Potential Jump: A Method for Rapid Electron Injection into Oxidoreductase Enzymes
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FT-IR Characterization of the Light-Induced Ni-L2 and Ni-L3 States of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F
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Electrochemical and Infrared Spectroscopic Studies Provide Insight into Reactions of the NiFe Regulatory Hydrogenase from Ralstonia eutropha with O2 and CO
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The Grateful Infrared: Sequential Protein Structural Changes Resolved by Infrared Difference Spectroscopy
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Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations
inferredcites →https://doi.org/10.1021/acscatal.6b03182openalex-snapshot
Proton Transfer in the Catalytic Cycle of [NiFe] Hydrogenases: Insight from Vibrational Spectroscopy
inferredcites →https://doi.org/10.1021/acscatal.6b03276openalex-snapshot
Pre-Steady-State Kinetics of Catalytic Intermediates of an [FeFe]-Hydrogenase
inferredcites →https://doi.org/10.1021/acscatal.9b02203openalex-snapshot
Geometry of the Catalytic Active Site in [FeFe]-Hydrogenase Is Determined by Hydrogen Bonding and Proton Transfer
inferredcites →https://doi.org/10.1021/ar500464jopenalex-snapshot
Measuring Electric Fields and Noncovalent Interactions Using the Vibrational Stark Effect
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Infrared Studies on the Interaction of Carbon Monoxide with Divalent Nickel in Hydrogenase from Chromatium vinosum
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Infrared Studies of the CO-Inhibited Form of the Fe-Only Hydrogenase fromClostridium pasteurianumI: Examination of Its Light Sensitivity at Cryogenic Temperatures
inferredcites →https://doi.org/10.1021/bi034235+openalex-snapshot
Attenuated Total Reflection Fourier Transform Infrared Spectroscopy: A Method of Choice for Studying Membrane Proteins and Lipids
inferredcites →https://doi.org/10.1021/bi034522dopenalex-snapshot
ATR-FTIR Spectroscopy of the PMand F Intermediates of Bovine andParacoccus denitrificansCytochromecOxidase
inferredcites →https://doi.org/10.1021/bi061114bopenalex-snapshot
Structural and Chemical Changes of the P M Intermediate of Paracoccus denitrificans Cytochrome c Oxidase Revealed by IR Spectroscopy with Labeled Tyrosines and Histidine
inferredcites →https://doi.org/10.1021/bi501391dopenalex-snapshot
Hybrid [FeFe]-Hydrogenases with Modified Active Sites Show Remarkable Residual Enzymatic Activity
inferredcites →https://doi.org/10.1021/bi701614wopenalex-snapshot
Time-Resolved ATR-FTIR Spectroscopy of the Oxygen Reaction in the D124N Mutant of Cytochrome c Oxidase from Paracoccus denitrificans
inferredcites →https://doi.org/10.1021/bi960392fopenalex-snapshot
A pH-Dependent Polarity Change at the Binuclear Center of Reduced Cytochrome c Oxidase Detected by FTIR Difference Spectroscopy of the CO Adduct
inferredcites →https://doi.org/10.1021/bi961522nopenalex-snapshot
Nanosecond Step-Scan FTIR Spectroscopy of Hemoglobin: Ligand Recombination and Protein Conformational Changes
inferredcites →https://doi.org/10.1021/bi9629079openalex-snapshot
Glutamate 286 in Cytochrome aa3 from Rhodobacter sphaeroides Is Involved in Proton Uptake during the Reaction of the Fully-Reduced Enzyme with Dioxygen
inferredcites →https://doi.org/10.1021/bi971813bopenalex-snapshot
Role of the Pathway through K(I-362) in Proton Transfer in Cytochrome c Oxidase from R. sphaeroides
inferredcites →https://doi.org/10.1021/bm070050xopenalex-snapshot
Effect of Water Content on the Structural Reorganization and Elastic Properties of Biopolymer Films: A Comparative Study
inferredcites →https://doi.org/10.1021/cr0204294openalex-snapshot
Water-Splitting Chemistry of Photosystem II
inferredcites →https://doi.org/10.1021/cr050191uopenalex-snapshot
Investigating and Exploiting the Electrocatalytic Properties of Hydrogenases
inferredcites →https://doi.org/10.1021/cr050196ropenalex-snapshot
Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
inferredcites →https://doi.org/10.1021/cr300463yopenalex-snapshot
Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO 2 Fixation
inferredcites →https://doi.org/10.1021/cr400641xopenalex-snapshot
Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage
inferredcites →https://doi.org/10.1021/cr500266aopenalex-snapshot
Reaction Mechanism of Cytochrome c Oxidase
inferredcites →https://doi.org/10.1021/cr60277a003openalex-snapshot
Hydride complexes of the transition metals
inferredcites →https://doi.org/10.1021/cr950057hopenalex-snapshot
Structure−Function Relationships of Alternative Nitrogenases
inferredcites →https://doi.org/10.1021/cr960436qopenalex-snapshot
Metal Activation of Enzymes in Nucleic Acid Biochemistry
inferredcites →https://doi.org/10.1021/ja00138a033openalex-snapshot
Investigation of CO bound to inhibited forms of nitrogenase MoFe protein by 13C ENDOR
inferredcites →https://doi.org/10.1021/ja00257a045openalex-snapshot
Vibrational mode structure and symmetry in proteins and analogs containing Fe4S4 clusters: resonance Raman evidence that HiPIP is tetrahedral while ferredoxin undergoes a D2d distortion
inferredcites →https://doi.org/10.1021/ja012645kopenalex-snapshot
Structural Studies of the Carbon Monoxide Complex of [NiFe]hydrogenase fromDesulfovibriovulgarisMiyazaki F: Suggestion for the Initial Activation Site for Dihydrogen
inferredcites →https://doi.org/10.1021/ja0169825openalex-snapshot
Decay of the Transient CuB−CO Complex Is Accompanied by Formation of the Heme Fe−CO Complex of Cytochrome cbb3−CO at Ambient Temperature: Evidence from Time-Resolved Fourier Transform Infrared Spectroscopy
inferredcites →https://doi.org/10.1021/ja021302zopenalex-snapshot
FTIR Detection of Protonation/Deprotonation of Key Carboxyl Side Chains Caused by Redox Change of the CuA-HemeaMoiety and Ligand Dissociation from the Hemea3-CuBCenter of Bovine Heart CytochromecOxidase
inferredcites →https://doi.org/10.1021/ja039320jopenalex-snapshot
Direct Detection of Formate Ligation in CytochromecOxidase by ATR-FTIR Spectroscopy
inferredcites →https://doi.org/10.1021/ja046818sopenalex-snapshot
Carbon Monoxide as an Intrinsic Ligand to Iron in the Active Site of the Iron−Sulfur-Cluster-Free Hydrogenase H 2 -Forming Methylenetetrahydromethanopterin Dehydrogenase As Revealed by Infrared Spectroscopy
inferredcites →https://doi.org/10.1021/ja971088sopenalex-snapshot
Time-Resolved Binding of Carbon Monoxide to Nitrogenase Monitored by Stopped-Flow Infrared Spectroscopy
inferredcites →https://doi.org/10.1021/ja9712837openalex-snapshot
Mössbauer and EPR Evidence for an All-Ferrous Fe4S4 Cluster with S = 4 in the Fe Protein of Nitrogenase
inferredcites →https://doi.org/10.1021/ja9715096openalex-snapshot
CO Binding to the FeMo Cofactor of CO-Inhibited Nitrogenase: 13CO and 1H Q-Band ENDOR Investigation
inferredcites →https://doi.org/10.1021/ja9943703openalex-snapshot
Photochemistry at the Active Site of the Carbon Monoxide Inhibited Form of the Iron-Only Hydrogenase (CpI)
inferredcites →https://doi.org/10.1021/jacs.5b01791openalex-snapshot
Proton-Coupled Electron Transfer Dynamics in the Catalytic Mechanism of a [NiFe]-Hydrogenase
inferredcites →https://doi.org/10.1021/jacs.6b12636openalex-snapshot
Proton Coupled Electronic Rearrangement within the H-Cluster as an Essential Step in the Catalytic Cycle of [FeFe] Hydrogenases
inferredcites →https://doi.org/10.1021/jacs.7b07548openalex-snapshot
Bridging Hydride at Reduced H-Cluster Species in [FeFe]-Hydrogenases Revealed by Infrared Spectroscopy, Isotope Editing, and Quantum Chemistry
inferredcites →https://doi.org/10.1021/jacs.8b04798openalex-snapshot
Mechanistic Exploitation of a Self-Repairing, Blocked Proton Transfer Pathway in an O2-Tolerant [NiFe]-Hydrogenase
inferredcites →https://doi.org/10.1021/jacs.9b08348openalex-snapshot
Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-Resolved Infrared Spectroscopy
inferredcites →https://doi.org/10.1021/jacs.9b09225openalex-snapshot
How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer
inferredcites →https://doi.org/10.1021/jacs.9b09745openalex-snapshot
Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates
inferredcites →https://doi.org/10.1021/jacs.9b13075openalex-snapshot
Shedding Light on Proton and Electron Dynamics in [FeFe] Hydrogenases
inferredcites →https://doi.org/10.1021/jp992329gopenalex-snapshot
Vibrational Stark Spectroscopy in Proteins: A Probe and Calibration for Electrostatic Fields
inferredcites →https://doi.org/10.1038/nature03921openalex-snapshot
A mechanistic principle for proton pumping by cytochrome c oxidase
inferredcites →https://doi.org/10.1038/nature04231openalex-snapshot
Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
inferredcites →https://doi.org/10.1038/nature10505openalex-snapshot
The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre
inferredcites →https://doi.org/10.1038/nature12239openalex-snapshot
Biomimetic assembly and activation of [FeFe]-hydrogenases
inferredcites →https://doi.org/10.1038/nature14110openalex-snapshot
Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase
inferredcites →https://doi.org/10.1038/nchembio.1311openalex-snapshot
Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic
inferredcites →https://doi.org/10.1038/ncomms16115openalex-snapshot
Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases
inferredcites →https://doi.org/10.1038/s41557-019-0266-1openalex-snapshot
A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor
inferredcites →https://doi.org/10.1038/s41570-020-0167-2openalex-snapshot
Methanogenesis involves direct hydride transfer from H2 to an organic substrate
inferredcites →https://doi.org/10.1039/b702328fopenalex-snapshot
Methods to probe protein transitions with ATR infrared spectroscopy
inferredcites →https://doi.org/10.1039/c3cp00119aopenalex-snapshot
Attenuated total reflectance infrared spectroelectrochemistry at a carbon particle electrode; unmediated redox control of a [NiFe]-hydrogenase solution
inferredcites →https://doi.org/10.1039/c6sc01098aopenalex-snapshot
Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution
inferredcites →https://doi.org/10.1039/c6sc02860hopenalex-snapshot
Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding
inferredcites →https://doi.org/10.1039/c7cp04757fopenalex-snapshot
Protonation/reduction dynamics at the [4Fe–4S] cluster of the hydrogen-forming cofactor in [FeFe]-hydrogenases
inferredcites →https://doi.org/10.1039/c7dt03785fopenalex-snapshot
Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity
inferredcites →https://doi.org/10.1039/c7dt04910bopenalex-snapshot
Comprehensive reaction mechanisms at and near the Ni–Fe active sites of [NiFe] hydrogenases
inferredcites →https://doi.org/10.1039/c7ee01738copenalex-snapshot
Balancing electron transfer rate and driving force for efficient photocatalytic hydrogen production in CdSe/CdS nanorod–[NiFe] hydrogenase assemblies
inferredcites →https://doi.org/10.1039/c9sc03717aopenalex-snapshot
Discovery of novel [FeFe]-hydrogenases for biocatalytic H 2 -production
inferredcites →https://doi.org/10.1039/d0sc00512fopenalex-snapshot
Spectroscopic investigations under whole-cell conditions provide new insight into the metal hydride chemistry of [FeFe]-hydrogenase
inferredcites →https://doi.org/10.1039/d0sc03319gopenalex-snapshot
Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture
inferredcites →https://doi.org/10.1039/d1dt00110hopenalex-snapshot
Site-selective protonation of the one-electron reduced cofactor in [FeFe]-hydrogenase
inferredcites →https://doi.org/10.1042/bst20130087openalex-snapshot
IR signatures of the metal centres of bovine cytochrome c oxidase: assignments and redox-linkage
inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03920.xopenalex-snapshot
UV‐A/blue‐light inactivation of the ‘metal‐free’ hydrogenase (Hmd) from methanogenic archaea
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A low‐spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]‐hydrogenases
inferredcites →https://doi.org/10.1073/pnas.0802512105openalex-snapshot
The proton donor for OO bond scission by cytochrome c oxidase
inferredcites →https://doi.org/10.1073/pnas.1010974107openalex-snapshot
Initiation of the proton pump of cytochrome c oxidase
inferredcites →https://doi.org/10.1073/pnas.1019419108openalex-snapshot
Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy
inferredcites →https://doi.org/10.1073/pnas.1114660108openalex-snapshot
Solar hydrogen-producing bionanodevice outperforms natural photosynthesis
inferredcites →https://doi.org/10.1073/pnas.1331436100openalex-snapshot
A simple energy-conserving system: Proton reduction coupled to proton translocation
inferredcites →https://doi.org/10.1073/pnas.1509277112openalex-snapshot
Key bioactive reaction products of the NO/H 2 S interaction are S/N-hybrid species, polysulfides, and nitroxyl
inferredcites →https://doi.org/10.1073/pnas.1530408100openalex-snapshot
Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase
inferredcites →https://doi.org/10.1073/pnas.1606178113openalex-snapshot
Stepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamics
inferredcites →https://doi.org/10.1073/pnas.1705628114openalex-snapshot
Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
inferredcites →https://doi.org/10.1073/pnas.96.26.14718openalex-snapshot
The heme-copper oxidases of Thermus thermophilus catalyze the reduction of nitric oxide: Evolutionary implications
inferredcites →https://doi.org/10.1074/jbc.274.6.3331openalex-snapshot
Carbon Monoxide and Cyanide as Intrinsic Ligands to Iron in the Active Site of [NiFe]-Hydrogenases
inferredcites →https://doi.org/10.1074/jbc.m117.788125openalex-snapshot
Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis
inferredcites →https://doi.org/10.1074/jbc.m803511200openalex-snapshot
The Protonation State of the Cross-linked Tyrosine during the Catalytic Cycle of Cytochrome c Oxidase
inferredcites →https://doi.org/10.1074/jbc.ra120.013091openalex-snapshot
In-cell infrared difference spectroscopy of LOV photoreceptors reveals structural responses to light altered in living cells
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/10.1126/sciadv.abg4474openalex-snapshot
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
inferredcites →https://doi.org/10.1126/science.284.5413.473openalex-snapshot
A Steric Mechanism for Inhibition of CO Binding to Heme Proteins
inferredcites →https://doi.org/10.1126/science.abc3183openalex-snapshot
Using nature’s blueprint to expand catalysis with Earth-abundant metals
inferredcites →https://doi.org/10.1146/annurev.bi.45.070176.001323openalex-snapshot
Calcium-Binding Proteins
inferredcites →https://doi.org/10.1366/0003702934067478openalex-snapshot
Surface-Enhanced Infrared Spectroscopy: The Origin of the Absorption Enhancement and Band Selection Rule in the Infrared Spectra of Molecules Adsorbed on Fine Metal Particles
inferredcites →https://doi.org/10.1366/0003702963905907openalex-snapshot
Atr/Ft-Ir Difference Spectroscopy of Biological Matter with Microsecond Time Resolution
inferredcites →https://doi.org/10.17169/refubium-6966openalex-snapshot
Protonation and Reduction Dynamics in [FeFe]-Hydrogenases
inferredcites →https://doi.org/10.3389/fchem.2021.669452openalex-snapshot
Quantification of Local Electric Field Changes at the Active Site of Cytochrome c Oxidase by Fourier Transform Infrared Spectroelectrochemical Titrations
inferredcites →https://doi.org/10.3390/catal8110530openalex-snapshot
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What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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