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 E-Mail An international research team from the Photobiotechnology Research Group at Ruhr-Universität Bochum (RUB) led by Professor Thomas Happe and the Laboratoire de Bioénergétique et Ingénierie des Protéines (CNRS) in Marseille has been able to get to the bottom of this unique feature. They describe the molecular mechanism in Nature Communications on 2 February 2021. Enzyme repeatedly survives the attack unharmed Representatives of the [FeFe]-hydrogenase enzyme group combine protons and electrons to form molecular hydrogen at particularly high turnover rates. Some of them even use sunlight as a primary energy source for this. However, even low oxygen concentrations quickly lead to the irreversible breakdown of the catalytic cofactor, called the H-cluster. This has so far been observed in all representatives of this enzyme group - except for CbA5H. This enzyme has a molecular mechanism that allows it to repeatedly survive the oxygen attack unharmed, says Thomas Happe.

Eckhard hofmannMartin winklerThomas happeJifu duanPhotobiotechnology research groupNature communicationsPhotobiotechnology research group at ruhr universitProfessor thomas happeLaboratoire de bioDes protProfessor eckhard hofmannProtein crystallographyPhotobiotechnology researchஎக்கர்த் ஹாஃப்மேன்மார்டின் விங்க்லர்தாமஸ் மகிழ்ச்சி