Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding.

ABSTRACT: 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 FeMo-cofactor to be established. Reduction of protons to H₂ is catalyzed by the wild type MoFe protein and β-98^Tyr→His and β-99^Phe→His variants of the MoFe protein at potentials more negative than -800 mV (vs. SHE), with greater electrocatalytic proton reduction rates observed for the variants compared to the wild type protein. Electrocatalytic proton reduction is strongly attenuated by carbon monoxide (CO), and the potential-dependence of CO binding to the

SUBMITTER: Paengnakorn P 

PROVIDER: S-EPMC5460594 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature