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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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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/ange.201209732openalex-snapshot
Resonanz‐Raman‐Spektroskopie als Methode zur Untersuchung des aktiven Zentrums von Hydrogenasen
inferredcites →https://doi.org/10.1002/ange.201408552openalex-snapshot
Control of the Transition between Ni‐C and Ni‐SIa States by the Redox State of the Proximal FeS Cluster in the Catalytic Cycle of [NiFe] Hydrogenase
inferredcites →https://doi.org/10.1002/ange.201502338openalex-snapshot
Infrared Spectroscopy During Electrocatalytic Turnover Reveals the Ni‐L Active Site State During H2 Oxidation by a NiFe Hydrogenase
inferredcites →https://doi.org/10.1002/anie.201209732openalex-snapshot
Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases
inferredcites →https://doi.org/10.1002/anie.201408552openalex-snapshot
Control of the Transition between Ni‐C and Ni‐SIa States by the Redox State of the Proximal FeS Cluster in the Catalytic Cycle of [NiFe] Hydrogenase
inferredcites →https://doi.org/10.1002/anie.201502338openalex-snapshot
Infrared Spectroscopy During Electrocatalytic Turnover Reveals the Ni‐L Active Site State During H2 Oxidation by a NiFe Hydrogenase
inferredcites →https://doi.org/10.1002/prot.21588openalex-snapshot
Proton pathways in a [NiFe]‐hydrogenase: A theoretical study
inferredcites →https://doi.org/10.1002/prot.22045openalex-snapshot
A QM/MM study of proton transport pathways in a [NiFe] hydrogenase
inferredcites →https://doi.org/10.1007/s00775-016-1348-9openalex-snapshot
Protonation states of intermediates in the reaction mechanism of [NiFe] hydrogenase studied by computational methods
inferredcites →https://doi.org/10.1016/s0969-2126(97)00313-4openalex-snapshot
Unusual ligand structure in Ni–Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis
inferredcites →https://doi.org/10.1017/s0033583502003815openalex-snapshot
What vibrations tell about proteins
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Guiding Principles of Hydrogenase Catalysis Instigated and Clarified by Protein Film Electrochemistry
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Applications of Photogating and Time Resolved Spectroscopy to Mechanistic Studies of Hydrogenases
inferredcites →https://doi.org/10.1021/acs.chemrev.6b00180openalex-snapshot
Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides
inferredcites →https://doi.org/10.1021/acs.jpcb.5b03075openalex-snapshot
FT-IR Characterization of the Light-Induced Ni-L2 and Ni-L3 States of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F
inferredcites →https://doi.org/10.1021/acs.jpcb.9b00617openalex-snapshot
Proton Transfer Pathways between Active Sites and Proximal Clusters in the Membrane-Bound [NiFe] Hydrogenase
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/bi501243yopenalex-snapshot
Comparison of the Structural Changes Occurring during the Primary Phototransition of Two Different Channelrhodopsins from Chlamydomonas Algae
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Theory of Coupled Electron and Proton Transfer Reactions
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Studies of virus structure by Raman spectroscopy. Cysteine conformation and sulfhydryl interactions in proteins and viruses. 1. Correlation of the Raman sulfur-hydrogen band with hydrogen bonding and intramolecular geometry in model compounds
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Direct Observation of the Bridged Water Stretching Vibrations Inside a Protein
inferredcites →https://doi.org/10.1021/ja005808yopenalex-snapshot
Relativistic DFT Calculations of the Paramagnetic Intermediates of [NiFe] Hydrogenase. Implications for the Enzymatic Mechanism
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/ja027522uopenalex-snapshot
Single Crystal EPR Studies of the Reduced Active Site of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F
inferredcites →https://doi.org/10.1021/ja036624xopenalex-snapshot
Direct Detection of a Hydrogen Ligand in the [NiFe] Center of the Regulatory H2-Sensing Hydrogenase fromRalstoniaeutrophain Its Reduced State by HYSCORE and ENDOR Spectroscopy
inferredcites →https://doi.org/10.1021/ja309563popenalex-snapshot
A Functional [NiFe]-Hydrogenase Model Compound That Undergoes Biologically Relevant Reversible Thiolate Protonation
inferredcites →https://doi.org/10.1021/ja3115899openalex-snapshot
A Metal–Metal Bond in the Light-Induced State of [NiFe] Hydrogenases with Relevance to Hydrogen Evolution
inferredcites →https://doi.org/10.1021/ja980837iopenalex-snapshot
Cysteine S−H as a Hydrogen-Bonding Probe in Proteins
inferredcites →https://doi.org/10.1021/jacs.5b00749openalex-snapshot
Ligand-Induced Proton Transfer and Low-Barrier Hydrogen Bond Revealed by X-ray Crystallography
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.5b03182openalex-snapshot
Discovery of Dark pH-Dependent H+ Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate
inferredcites →https://doi.org/10.1021/jacs.6b07789openalex-snapshot
Glutamate Gated Proton-Coupled Electron Transfer Activity of a [NiFe]-Hydrogenase
inferredcites →https://doi.org/10.1021/jacs.7b03611openalex-snapshot
Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site
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.8b06996openalex-snapshot
Terminal Thiolate-Dominated H/D Exchanges and H2 Release: Diiron Thiol–Hydride
inferredcites →https://doi.org/10.1021/jp801151kopenalex-snapshot
Correlation between the Hydrogen-Bond Structures and the C═O Stretching Frequencies of Carboxylic Acids as Studied by Density Functional Theory Calculations: Theoretical Basis for Interpretation of Infrared Bands of Carboxylic Groups in Proteins
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.1500openalex-snapshot
Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase
inferredcites →https://doi.org/10.1038/nchembio.1976openalex-snapshot
Mechanism of Hydrogen activation by NiFe-hydrogenases
inferredcites →https://doi.org/10.1039/c6cp04628bopenalex-snapshot
Photoactivation of the Ni-SI r state to the Ni-SI a state in [NiFe] hydrogenase: FT-IR study on the light reactivity of the ready Ni-SI r state and as-isolated enzyme revisited
inferredcites →https://doi.org/10.1039/c7cc06061kopenalex-snapshot
Equilibrium between inactive ready Ni-SI r and active Ni-SI a states of [NiFe] hydrogenase studied by utilizing Ni-SI r -to-Ni-SI a photoactivation
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/10.1074/jbc.m114.634840openalex-snapshot
Proton Transfers in a Channelrhodopsin-1 Studied by Fourier Transform Infrared (FTIR) Difference Spectroscopy and Site-directed Mutagenesis
inferredcites →https://doi.org/10.1074/jbc.m312716200openalex-snapshot
A Glutamate Is the Essential Proton Transfer Gate during the Catalytic Cycle of the [NiFe] Hydrogenase
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