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Synthetic Models for Nickel-Iron Hydrogenase Featuring Redox-Active Ligands
David Schilter
,
Danielle L. Gray
, Amy L. Fuller
,
Thomas B. Rauchfuss
School of Chemical Sciences
Chemistry
Research output
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peer-review
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Keyphrases
Dithiolate
100%
Synthetic Model
100%
Iron-nickel Alloy
100%
Redox-active Ligands
100%
Iron Hydrogenase
100%
Diphosphine
75%
Ferrocene
75%
Ferrocenyl Phosphine
75%
CO 2
50%
Phosphine
50%
Hydrogenase
25%
Hydrides
25%
Hydride Species
25%
Proton Relay
25%
Proton
25%
Active Sites
25%
Redox State
25%
Iron-sulfur Cluster
25%
Redox-active Moieties
25%
Redox-active
25%
Hydrogen Evolution
25%
Dihydrogen
25%
Redox Protein
25%
Ni(II)
25%
Iron-sulfur
25%
Protein Features
25%
Active Auxiliary
25%
Ferrocenyl Group
25%
Mixed-valent Complexes
25%
Chemistry
Hydrogenase
100%
Ferrocene
100%
Dihydrogen
33%
Hydrogen
33%
Redox State
33%
Iron-Sulfur Cluster
33%
Cofactor
33%