Journal
INORGANIC CHEMISTRY
Volume 60, Issue 13, Pages 9233-9237Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.inorgchem.1c00940
Keywords
-
Categories
Funding
- National Institutes of Health [R01-GM-057378]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
Ask authors/readers for more resources
Two new desoxo molybdenum(V) complexes have been synthesized as models for the paramagnetic high-g split intermediate in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR). The geometric and electronic structures of high-g split and other EPR-active type II/III DMSOR family enzyme forms have been characterized using EXAFS and EPR data, supporting a specific 6-coordinate structure for the high-g split.
Two new desoxo molybdenum(V) complexes have been synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR). Extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data are used to provide new insight into the geometric and electronic structures of high-g split and other EPR-active type II/III DMSOR family enzyme forms. The results support a 6-coordinate [(PDT)(2)Mo(OH)(O-Ser)](-) structure (PDT = pyranopterin dithiolene) for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available