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: | , , , , , , , |
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| Format: | Journal article |
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Royal Society of Chemistry
2016
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| _version_ | 1797104469924642816 |
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| author | Paengnakorn, P Ash, P Shaw, S Danyal, K Chen, T Dean, D Seefeldt, L Vincent, K |
| author_facet | Paengnakorn, P Ash, P Shaw, S Danyal, K Chen, T Dean, D Seefeldt, L Vincent, K |
| author_sort | Paengnakorn, P |
| collection | OXFORD |
| description | 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-98Tyr→His and β 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. |
| first_indexed | 2024-03-07T06:34:15Z |
| format | Journal article |
| id | oxford-uuid:f71041f2-d380-48f1-b03a-92e0837e1c53 |
| institution | University of Oxford |
| last_indexed | 2024-03-07T06:34:15Z |
| publishDate | 2016 |
| publisher | Royal Society of Chemistry |
| record_format | dspace |
| spelling | oxford-uuid:f71041f2-d380-48f1-b03a-92e0837e1c532022-03-27T12:39:53ZInfrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO bindingJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f71041f2-d380-48f1-b03a-92e0837e1c53Symplectic Elements at OxfordRoyal Society of Chemistry2016Paengnakorn, PAsh, PShaw, SDanyal, KChen, TDean, DSeefeldt, LVincent, KWe 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-98Tyr→His and β 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. |
| spellingShingle | Paengnakorn, P Ash, P Shaw, S Danyal, K Chen, T Dean, D Seefeldt, L Vincent, K Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding |
| title | Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding |
| title_full | Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding |
| title_fullStr | Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding |
| title_full_unstemmed | Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding |
| title_short | Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding |
| title_sort | infrared spectroscopy of the nitrogenase mofe protein under electrochemical control potential triggered co binding |
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