期刊
INORGANIC CHEMISTRY
卷 51, 期 3, 页码 1408-1418出版社
AMER CHEMICAL SOC
DOI: 10.1021/ic201643t
关键词
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资金
- NIH [GM-37773, S10RR020959]
- US-Israel Binational Science Foundation [2006179]
- NSF [DBI-0139459, DBI-9604939, BIR-9224431]
- Direct For Education and Human Resources
- Division Of Research On Learning [2006179] Funding Source: National Science Foundation
In our previous study of the fatal R160Q mutant of human sulfite oxidase (hSO) at low pH (Astashkin et al. J. Am. Chem. Soc. 2008, 130, 8471-8480), a new Mo(V) species, denoted species 1, was observed at low pH values. Species 1 was ascribed to a six-coordinate Mo(V) center with an exchangeable terminal oxo ligand and an equatorial sulfate group on the basis of pulsed EPR spectroscopy and S-33 and O-17 labeling. Here we report new results for species 1 of R160Q based on substitution of the sulfur-containing ligand by a phosphate group, pulsed EPR spectroscopy in K-a- and W-bands, and extensive density functional theory (DFT) calculations applied to large, more realistic molecular models of the enzyme active site. The combined results unambiguously show that species 1 has an equatorial sulfite as the only exchangeable ligand. The two types of O-17 signals that are observed arise from the coordinated and remote oxygen atoms of the sulfite ligand. A typical five-coordinate Mo(V) site is compatible with the observed and calculated EPR parameters.
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