Thomas Happe

This paper characterizes SoHydAB, a [FeFe]-hydrogenase in Shewanella oneidensis, showing its unique electron acceptor and metabolic role in formate oxidation.

This study investigates how substituting the azadithiolate ligand in ToHydA affects O2-stability by preventing the formation of specific states and altering structural dynamics.

This study identifies a histidine-mediated pendulum mechanism in [FeFe]-hydrogenases that enhances catalytic activity by facilitating proton transfer.

The paper presents a high-resolution crystal structure of CbA5H in the O2-stable Hinact state, showing direct thiol binding to the active site iron, supported by DFT calculations.

This study uses molecular simulations and mutagenesis to investigate the role of an additional cysteine in enhancing H2 production activity of ToHydA without affecting O2 stability.

This study identifies ToHydA, an O2-stable [FeFe]-hydrogenase from Thermosediminibacter oceani, and reveals structural features that protect the H-cluster from O2-induced degradation.