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Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from <i>E. coli</i> reveals the role of the protein scaffold in controlling the active site environment

Solomon L. D. Wrathall, Barbara Procacci, Marius Horch, Emily Saxton, Chris Furlan, Julia Walton, Yvonne Rippers, James N. Blaza, Gregory M. Greetham, Michael Towrie, Anthony W. Parker, Jason M. Lynam, Alison Parkin, Neil T. Hunt

2022Physical Chemistry Chemical Physics13 citationsDOIOpen Access PDF

Abstract

] in aqueous solution and conclude that the protein scaffold creates a unique biomolecular environment for the NiFe site that cannot be represented by analogy to simple models of solvation.

Topics & Concepts

Active siteScaffold proteinSpectroscopyUltrashort pulseChemistryScaffoldHydrogenaseEscherichia coliInfrared spectroscopyNear-infrared spectroscopyCrystallographyMaterials scienceBiophysicsBiochemistryEnzymeBiologyOrganic chemistryPhysicsGeneOpticsLaserBiomedical engineeringMedicineQuantum mechanicsSignal transductionMetalloenzymes and iron-sulfur proteinsElectrocatalysts for Energy ConversionSpectroscopy and Quantum Chemical Studies
Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from <i>E. coli</i> reveals the role of the protein scaffold in controlling the active site environment | Litcius