Journal article
C. K. Arya, S. Yadav, Jonathan A Fine, A. Casañal, G. Chopra, G. Ramanathan, K. Vinothkumar, R. Subramanian
Angewandte Chemie, 2020
Angewandte Chemie, 2020
Semantic Scholar
DOI
PubMedCentral
PubMed
Cite
Cite
APA
Click to copy
Arya, C. K., Yadav, S., Fine, J. A., Casañal, A., Chopra, G., Ramanathan, G., … Subramanian, R. (2020). A 2‐Tyr‐1‐carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase. Angewandte Chemie.
Chicago/Turabian
Click to copy
Arya, C. K., S. Yadav, Jonathan A Fine, A. Casañal, G. Chopra, G. Ramanathan, K. Vinothkumar, and R. Subramanian. “A 2‐Tyr‐1‐Carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase.” Angewandte Chemie (2020).
MLA
Click to copy
Arya, C. K., et al. “A 2‐Tyr‐1‐Carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase.” Angewandte Chemie, 2020.
BibTeX Click to copy
@article{c2020a,
title = {A 2‐Tyr‐1‐carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase},
year = {2020},
journal = {Angewandte Chemie},
author = {Arya, C. K. and Yadav, S. and Fine, Jonathan A and Casañal, A. and Chopra, G. and Ramanathan, G. and Vinothkumar, K. and Subramanian, R.}
}
Abstract
Abstract N,N‐dimethyl formamide (DMF) is an extensively used organic solvent but is also a potent pollutant. Certain bacterial species from genera such as Paracoccus, Pseudomonas, and Alcaligenes have evolved to use DMF as a sole carbon and nitrogen source for growth via degradation by a dimethylformamidase (DMFase). We show that DMFase from Paracoccus sp. strain DMF is a halophilic and thermostable enzyme comprising a multimeric complex of the α2β2 or (α2β2)2 type. One of the three domains of the large subunit and the small subunit are hitherto undescribed protein folds of unknown evolutionary origin. The active site consists of a mononuclear iron coordinated by two Tyr side‐chain phenolates and one carboxylate from Glu. The Fe3+ ion in the active site catalyzes the hydrolytic cleavage of the amide bond in DMF. Kinetic characterization reveals that the enzyme shows cooperativity between subunits, and mutagenesis and structural data provide clues to the catalytic mechanism.
