State-of-the-Art in Molybdenum Cofactor Research

Dear Colleagues,

The pterin-based molybdenum cofactor (Moco) and the iron-molybdenum cofactor (FeMoco) of nitrogenase are old inventions of nature. LUCA, the last universal common ancestor of a living cell, was able to synthesize these essential prosthetic groups. Bacteria host over fifty molybdenum enzymes, while eukaryotes only host five. Loss of Moco biosynthesis is lethal for most organisms.

This Special Issue aims at illustrating the most recent and pertinent developments in Moco and FeMoco research in eukaryotic organisms and in bacteria, respectively. This will include the biosynthesis pathways of both cofactors, molybdenum uptake in cells, the mechanisms of insertion of molybdenum into the cofactor scaffolds, the carrier and storage proteins of Moco following its biosynthesis, and the insertion of cofactors into their target enzymes. Special attention will be paid to the areas of Moco and FeMoco spectroscopy, model compound chemistry, chemical synthesis of Moco, and the structural biology of Moco and FeMoco. The key role of human Moco deficiency and its therapy will also be highlighted. We are not focusing on molybdenum enzymes with their function, biochemistry, and their structural biology.

Communications, full papers, and reviews on the abovementioned topics are particularly welcome.

Prof. Dr. Ralf-Rainer Mendel
Dr. Tobias Kruse
Guest Editors

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