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

Journal Article · · Chemical Science
DOI:https://doi.org/10.1039/c6sc02860h· OSTI ID:1624942
 [1];  [2];  [3];  [3];  [2];  [4];  [3];  [2]
  1. Univ. of Oxford (United Kingdom). Inorganic Chemistry Lab. Dept. of Chemistry; DOE/OSTI
  2. Univ. of Oxford (United Kingdom). Inorganic Chemistry Lab. Dept. of Chemistry
  3. Utah State Univ., Logan, UT (United States). Dept. of Chemistry and Biochemistry
  4. Virginia Polytechnic Inst. and State Univ. (Virginia Tech), Blacksburg, VA (United States). Fralin Center. Dept. of Biochemistry
+ Show Author Affiliations
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 b-98Tyr/His and b-99Phe/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 FeMo-cofactor is determined by in situ infrared (IR) spectroelectrochemistry. The vibrational wavenumbers for CO coordinated to the FeMo-cofactor are consistent with earlier IR studies on the MoFe protein with Fe protein/ATP as reductant showing that electrochemically generated states of the protein are closely related to states generated with the native Fe protein as electron donor.
Research Organization:
Virginia Polytechnic Inst. and State Univ. (Virginia Tech), Blacksburg, VA (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
Grant/Contract Number:
SC0010687
OSTI ID:
1624942
Journal Information:
Chemical Science, Journal Name: Chemical Science Journal Issue: 2 Vol. 8; ISSN 2041-6520; ISSN CSHCBM
Publisher:
Royal Society of ChemistryCopyright Statement
Country of Publication:
United States
Language:
English

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Bioelectrochemical Haber-Bosch Process: An Ammonia-Producing H 2 /N 2 Fuel Cell journal February 2017
Pyrene‐Based Noncovalent Immobilization of Nitrogenase on Carbon Surfaces journal January 2020
Nitrogen Reduction to Ammonia on a Biomimetic Mononuclear Iron Centre: Insights into the Nitrogenase Enzyme journal December 2017
Electrochemical and spectroscopic methods for evaluating molecular electrocatalysts journal May 2017
Comparison of hydroxycarboxylato imidazole molybdenum( iv ) complexes and nitrogenase protein structures: indirect evidence for the protonation of homocitrato FeMo-cofactors journal January 2018
Spectroelectrochemistry, the future of visualizing electrode processes by hyphenating electrochemistry with spectroscopic techniques journal January 2020
Beyond fossil fuel–driven nitrogen transformations journal May 2018

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