Resonance Raman spectroscopy of pyranopterin molybdenum enzymes

Resonance Raman spectroscopy (rR) is a powerful spectroscopic probe that is widely used for studying the geometric and electronic structure of metalloproteins. In this focused review, we detail how resonance Raman spectroscopy has contributed to a greater understanding of electronic structure, geometric structure, and the reaction mechanisms of pyranopterin molybdenum enzymes. The review focuses on the enzymes sulfite oxidase (SO), dimethyl sulfoxide reductase (DMSOR), xanthine oxidase (XO), and carbon monoxide dehydrogenase. Specifically, we highlight how Mo-O-oxo, Mo-S-sulfido, Mo-S-dithiolene, and dithiolene C=C vibrational modes, isotope and heavy atom perturbations, resonance enhancement, and associated Raman studies of small molecule analogs have provided detailed insight into the nature of these metalloenzyme active sites.

Automated summary

Resonance Raman spectroscopy is a powerful tool for studying the geometric and electronic structure of metalloproteins. This review focuses on the enzymes sulfite oxidase, dimethyl sulfoxide reductase, xanthine oxidase, and carbon monoxide dehydrogenase, and highlights how resonance Raman studies have provided detailed insight into the nature of these metalloenzyme active sites.