Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases

Bigna Wörsdörfer, Mahesh Lingaraju, Neela H. Yennawar, Amie K. Boal, Carsten Krebs, J. Martin Bollinger, Maria Eirini Pandelia

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

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 Mössbauer 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.

Original languageEnglish (US)
Pages (from-to)18874-18879
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume110
Issue number47
DOIs
StatePublished - Nov 19 2013

All Science Journal Classification (ASJC) codes

  • General

Fingerprint Dive into the research topics of 'Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases'. Together they form a unique fingerprint.

Cite this