ChemRxiv
These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
1/1
3 files

Following Electroenzymatic Hydrogen Production by Rotating Ring Disk Electrochemistry and Mass Spectrometry

preprint
submitted on 18.01.2021, 09:13 and posted on 19.01.2021, 06:17 by Jaloliddin Khushvakov, Robin Nussbaum, Cécile Cadoux, Jifu Duan, Sven T. Stripp, Ross Milton

We report on two new approaches to study H2-producing metalloenzymes using electrochemistry and mass spectrometry, where H+ reduction is driven by hydrogenase within an electrochemically active polymer (redox polymer). Researchers have established electrochemical approaches to utilize the H2-processing metalloenzyme hydrogenase at electrode surfaces. However, it is more-than-often the case that hydrogenase electrodes are employed for H2 oxidation. There is significant interest in using renewable electrical energy to drive low-potential reductive reactions such as H2 evolution and N2 fixation, particularly with metalloenzymes. However, much work is required to understand metalloenzymes.

The use of rotating ring disk electrochemistry with hydrogenase is innovative in that it provides a live method to quantify the H2 being produced by the enzyme. This method will be valuable in determining product distributions for such enzymes in real-time, at electrode surfaces.

There is also significant interest in utilizing isotopes of enzymatic substrates when performing electrochemistry, since the rate of the reaction corresponds to the current at the electrode. However, researchers of electroenzymatic H+ reduction have yet to utilize online mass spectrometry to analyze the products of hydron reduction. We report on the ability to follow and differentiate the formation of H2, HD and D2 in real-time, permitting the calculation of apparent kinetic isotope effects. This approach will be valuable to characterizing rate-limiting steps involving H+, as well as for other gas-processing metalloenzymes.

Funding

Deutsche Forschungsgemeinschaft 1927 (1554/5-1)

COMAD University of Geneva

Ernest Boninchi Foundation

Société Académique de Genève

Fondation Ernst et Lucie Schmidheiny

History

Email Address of Submitting Author

ross.milton@unige.ch

Institution

University of Geneva

Country

Switzerland

ORCID For Submitting Author

0000-0002-2229-0243

Declaration of Conflict of Interest

No conflicts of interest to declare

Exports