期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 47, 页码 18874-18879出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1315927110
关键词
nonheme diiron enzymes; C-H activation; superoxo intermediate; PhnY; structural genomics
资金
- National Science Foundation [MCB1330784]
- National Institutes of Health Pathway to Independence [K99/R00]
- US Department of Energy (DOE) Office of Science by Argonne National Laboratory
- US DOE [DEAC02- 06CH11357]
- Michigan Economic Development Corporation and Michigan Technology Tri-Corridor [085P1000817]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1330784] Funding Source: National Science Foundation
The founding members of the HD-domain protein superfamily are phosphohydrolases, and newly discovered members are generally annotated as such. However, myo-inositol oxygenase (MIOX) exemplifies a second, very different function that has evolved within the common scaffold of this superfamily. A recently discovered HD protein, PhnZ, catalyzes conversion of 2-amino-1-hydroxyethylphosphonate to glycine and phosphate, culminating a bacterial pathway for the utilization of environmentally abundant 2-aminoethylphosphonate. Using Mssbauer and EPR spectroscopies, X-ray crystallography, and activity measurements, we show here that, like MIOX, PhnZ employs a mixed-valent FeII/FeIII cofactor for the O2-dependent oxidative cleavage of its substrate. Phylogenetic analysis suggests that many more HD proteins may catalyze yet-unknown oxygenation reactions using this hitherto exceptional FeII/FeIII cofactor. The results demonstrate that the catalytic repertoire of the HD superfamily extends well beyond phosphohydrolysis and suggest that the mechanism used by MIOX and PhnZ may be a common strategy for oxidative C-X bond cleavage.
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