Work

The unusual formaldehyde-induced activation of [NiFe]-hydrogenase: Implications from protein film electrochemistry and infrared spectroscopy

Year: 2025

Type: article

Abstract: Here we investigate how formaldehyde (HCHO), a known strong inhibitor of [FeFe]‑hydrogenases and a mild inhibitor of [NiFe]‑hydrogenases, may exert more complex effects on this group of metalloenzymes, which reversibly catalyze the 2H + /H₂ reaction. We investigated the [NiFe]‑hydrogenase Hyd-2 from E. coli using protein film electrochemistry, a technique that enables the measurement of enzyme activity when the enzyme is adequately adsorbed on the electrode. The effect of HCHO on the electrocatalytic performance of Hyd-2 is highly dependent on the buffer pH and the direction of catalysis. During H₂ production, HCHO consistently acts as an inhibitor of Hyd-2. However, this effect is reversed in acidic pH values, where HCHO can mildly enhance the electrocatalytic H₂ oxidation by Hyd-2. FTIR investigations did not detect any new redox intermediate resulting from the inhibition or activation. Therefore, we propose that HCHO - a natural electrophile that can readily react with nucleophiles and proton acceptors - may facilitate the transfer protons during the rapid transformation of different redox species participating in the catalytic cycle of [NiFe]‑hydrogenases.

Source: Bioelectrochemistry

DOI: 10.1016/j.bioelechem.2025.108974

Authors: Lei Wan, Yanxin Gao, Serena DeBeer, Olaf Rüdiger

Institutions: Nankai University, Max Planck Institute for Chemical Energy Conversion, State Key Laboratory of Medicinal Chemical Biology

Language: English

Topic: Metalloenzymes and iron-sulfur proteins

Subfield: Renewable Energy, Sustainability and the Environment

Field: Energy

Domain: Physical Sciences

SDG: Affordable and clean energy

Open Access status: hybrid

Estimated APC paid: $3,970