Corrigendum to "Transport limited adsorption experiments give a new lower estimate of the turnover frequency of hydrogenase 1" BBA Advances 3 (2023) 100090.

[This corrects the article DOI: 10.1016/j.bbadva.

A Chimeric NiFe Hydrogenase Heterodimer to Assess the Role of the Electron Transfer Chain in Tuning the Enzyme's Catalytic Bias and Oxygen Tolerance.

The observation that some homologous enzymes have the same active site but very different catalytic properties demonstrates the importance of long-range effects in enzyme catalysis, but these effects are often difficult to rationalize. The NiFe hydrogenases 1 and 2 (Hyd 1 and Hyd 2) from both consist of a large catalytic subunit that embeds the same dinuclear active site and a small electron-transfer subunit with a chain of three FeS clusters. Hyd 1 is mostly active in H oxidation and resistant to inhibitors, whereas Hyd 2 also catalyzes H production and is strongly inhibited by O and CO.

Transport limited adsorption experiments give a new lower estimate of the turnover frequency of hydrogenase 1.

Protein Film Electrochemistry is a technique in which a redox enzyme is directly wired to an electrode, which substitutes for the natural redox partner. In this technique, the electrical current flowing through the electrode is proportional to the catalytic activity of the enzyme. However, in most cases, the amount of enzyme molecules contributing to the current is unknown and the absolute turnover frequency cannot be determined.