tungsten enzymes
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Inorganics ◽  
2020 ◽  
Vol 8 (3) ◽  
pp. 19 ◽  
Author(s):  
Jing Yang ◽  
John H. Enemark ◽  
Martin L. Kirk

Here we highlight past work on metal–dithiolene interactions and how the unique electronic structure of the metal–dithiolene unit contributes to both the oxidative and reductive half reactions in pyranopterin molybdenum and tungsten enzymes. The metallodithiolene electronic structures detailed here were interrogated using multiple ground and excited state spectroscopic probes on the enzymes and their small molecule analogs. The spectroscopic results have been interpreted in the context of bonding and spectroscopic calculations, and the pseudo-Jahn–Teller effect. The dithiolene is a unique ligand with respect to its redox active nature, electronic synergy with the pyranopterin component of the molybdenum cofactor, and the ability to undergo chelate ring distortions that control covalency, reduction potential, and reactivity in pyranopterin molybdenum and tungsten enzymes.


2019 ◽  
Vol 394 ◽  
pp. 53-64 ◽  
Author(s):  
Cristina M. Cordas ◽  
José J.G. Moura

Author(s):  
Andrew M. Crawford ◽  
Julien J. H. Cotelesage ◽  
Roger C. Prince ◽  
Graham N. George

Author(s):  
Ulf Ryde ◽  
Geng Dong ◽  
Jilai Li ◽  
Milica Feldt ◽  
Ricardo A. Mata

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