Similar enzymes, different structures: Phthalate dioxygenase is an α3α3 stacked hexamer, not an α3β3 trimer like “normal” Rieske oxygenases
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference36 articles.
1. Aspartate 205 in the Catalytic Domain of Naphthalene Dioxygenase Is Essential for Activity
2. Histidine Ligand Protonation and Redox Potential in the Rieske Dioxygenases: Role of a Conserved Aspartate in Anthranilate 1,2-Dioxygenase
3. Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites
4. Substitutions of the “Bridging” Aspartate 178 Result in Profound Changes in the Reactivity of the Rieske Center of Phthalate Dioxygenase
5. The “Bridging” Aspartate 178 in Phthalate Dioxygenase Facilitates Interactions between the Rieske Center and the Iron(II)−Mononuclear Center
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3. Determining the impacts of environmental parameters on model microbial community dynamics isolated from Rustumihia WWTP/Iraq;IOP Conference Series: Materials Science and Engineering;2020-06-01
4. Biodegradation pathway of di-(2-ethylhexyl) phthalate by a novel Rhodococcus pyridinivorans XB and its bioaugmentation for remediation of DEHP contaminated soil;Science of The Total Environment;2018-11
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