Structural characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) fromSphingobium chlorophenolicum, a new type of aromatic ring-cleavage enzyme

Author:

Hayes Robert P.1,Green Abigail R.2,Nissen Mark S.1,Lewis Kevin M.1,Xun Luying2,Kang ChulHee12

Affiliation:

1. Department of Chemistry; Washington State University; Pullman WA 99164-4630 USA

2. School of Molecular Biosciences; Washington State University; Pullman WA 99164-4660 USA

Funder

NSF

M.J. Murdock Charitable Trust

Publisher

Wiley

Subject

Molecular Biology,Microbiology

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3. Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases;Arciero;J Biol Chem,1986

4. [17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases;Arciero;J Biol Chem,1985

5. 4-Hydroxyphenylpyruvate dioxygenase is an iron-tyrosinate protein;Bradley;J Biol Chem,1986

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