Document Type
Article
Version
Final Published Version
Publication Title
Molecules
Volume
28
Publication Date
2023
Abstract
The pyranopterin dithiolene ligand is remarkable in terms of its geometric and electronic structure and is uniquely found in mononuclear molybdenum and tungsten enzymes. The pyranopterindithiolene is found coordinated to the metal ion, deeply buried within the protein, and non-covalently attached to the protein via an extensive hydrogen bonding network that is enzyme specific.However, the function of pyranopterin dithiolene in enzymatic catalysis has been difficult to determine. This focused account aims to provide an overview of what has been learned from the study of pyranopterin dithiolene model complexes of molybdenum and how these results relate to the enzyme systems. This work begins with a summary of what is known about the pyranopterindithiolene ligand in the enzymes. We then introduce the development of inorganic small molecule complexes that model aspects of a coordinated pyranopterin dithiolene and discuss the results o fdetailed physical studies of the models by electronic absorption, resonance Raman, X-ray absorption and NMR spectroscopies, cyclic voltammetry, X-ray crystallography, and chemical reactivity.
Citation
Burgmayer, Sharon J. Nieter and Martin L. Kirk. 2023. "Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis." Molecules 28 (22): 7456. https://doi.org/10.3390/molecules28227456.
DOI
https://doi.org/10.3390/molecules28227456
