Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-Resolved Infrared Spectroscopy
Author:
Affiliation:
1. Department of Chemistry, Emory University, Atlanta, Georgia 30030, United States
2. Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany
Funder
Division of Chemistry
Max-Planck-Gesellschaft
Division of Materials Research
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.9b08348
Reference38 articles.
1. Hydrogenases
2. Oxygen-Tolerant H2 Production by [FeFe]-H2ase Active Site Mimics Aided by Second Sphere Proton Shuttle
3. A [RuRu] Analogue of an [FeFe]-Hydrogenase Traps the Key Hydride Intermediate of the Catalytic Cycle
4. A Mixed-Valent, Fe(II)Fe(I), Diiron Complex Reproduces the Unique Rotated State of the [FeFe]Hydrogenase Active Site
5. Going beyond Structure: Nickel-Substituted Rubredoxin as a Mechanistic Model for the [NiFe] Hydrogenases
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