Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding
We demonstrate electrochemical control of the nitrogenase MoFe protein, in the absence of Fe protein or ATP, using europium (III/II) polyaminocarboxylate complexes as electron transfer mediators. This allows the potential dependence of proton reduction and inhibitor (CO) binding to the active site F...
Main Authors: | Paengnakorn, P, Ash, P, Shaw, S, Danyal, K, Chen, T, Dean, D, Seefeldt, L, Vincent, K |
---|---|
Format: | Journal article |
Published: |
Royal Society of Chemistry
2016
|
Similar Items
-
IR spectroelectrochemical study of ligand binding to the metal centres of nitrogenase
by: Paengnakorn, P, et al.
Published: (2014) -
Uncoupling nitrogenase: catalytic reduction of hydrazine to ammonia by a MoFe protein in the absence of Fe protein-ATP.
by: Danyal, K, et al.
Published: (2010) -
Preparation of isotopically labeled MoFe protein of nitrogenase
by: Christie, Patricia Dianne, 1967-
Published: (2005) -
Fe protein docking transduces conformational changes to MoFe nitrogenase active site in a nucleotide-dependent manner
by: Monika Tokmina-Lukaszewska, et al.
Published: (2023-11-01) -
Electrochemical and IR spectroelectrochemical studies of ligand binding to the metal centres of nitrogenase
by: Paengnakorn, P
Published: (2014)