Work

Tuning the H 2 Production Activity of ToHydA by Molecular Simulation-Informed Protein Engineering

Year: 2026

Type: article

Abstract: ABSTRACT In the context of bio-hydrogen production, the O 2 -stable Group B [FeFe]-hydrogenase from Thermosediminibacter oceani has attracted significant interest due to its distinctive “TSCCCP” motif near the active site, which contains an additional (third) cysteine residue that is absent in the “TSCCP” motif of standard Group A hydrogenases. The precise role of the additional cysteine residue in H 2 production has remained an open question. In this study, we sought to contribute to the understanding of this cysteine’s role in H 2 production by combining molecular dynamics (MD) simulations, site-directed mutagenesis, biochemical assays, and Fourier-transform infrared (FTIR) spectroscopy. Remarkably, a cysteine-to-serine exchange variant (TSSCCP) demonstrated enhanced H 2 production activity without compromising the O 2 -stability of ToHydA, offering new insights into its functional dynamics.

Source: Biochemistry

DOI: 10.1021/acs.biochem.6c00006

Authors: Chandan K. Das, Subhasri Ghosh, Shuvankar Naskar, Thomas Happe, Lars V. Schäfer

Institutions: RWTH Aachen University, Ruhr University Bochum

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: green

Funders: Deutscher Akademischer Austauschdienst, Deutsche Forschungsgemeinschaft, Volkswagen Foundation