Asset Details
Do you wish to reserve the book?
Investigating the quaternary structure of a homomultimeric catechol 1,2-dioxygenase: An integrative structural biology study
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Investigating the quaternary structure of a homomultimeric catechol 1,2-dioxygenase: An integrative structural biology study
Do you wish to request the book?
Investigating the quaternary structure of a homomultimeric catechol 1,2-dioxygenase: An integrative structural biology study
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Investigating the quaternary structure of a homomultimeric catechol 1,2-dioxygenase: An integrative structural biology study
2025
Overview
The structural analysis of catechol 1,2 dioxygenase from Stutzerimonas frequens GOM2, SfC12DO, was conducted using various structural techniques. SEC-SAXS experiments revealed that SfC12DO, after lyophilization and reconstitution processes, can form multiple enzymatically active oligomers, including dimers, tetramers, and octamers. These findings differ from previous studies, which reported active dimers in homologous counterparts with available crystallographic structures, or trimers observed exclusively in solution for SfC12DO and its homologous isoA C12DO from Acinetobacter radioresistens under low ionic strength conditions. In some cases, tetramers were also reported, such as for the Rodococcus erythropolis C12DO. The combined results of Small-Angle X-ray Scattering, Dynamic Light Scattering, and Transmission Electron Microscopy experiments provided additional insights into these active oligomers’ shape and molecular organization in an aqueous solution. These results highlight the oligomeric structural plasticity of SfC12DO, proving that it can exist in different oligomeric forms depending on the physicochemical characteristics of the solutions in which the experiments were performed. Remarkably, regardless of its oligomeric state, SfC12DO maintains its enzymatic activity even after prior lyophilization. All these characteristics make SfC12DO a putative candidate for bioremediation applications in polluted soils or waters.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Analysis
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Catechin
/ Catechol
/ Catechol 1,2-Dioxygenase - chemistry
/ Catechol 1,2-Dioxygenase - metabolism
/ Crystals
/ Dimers
/ E coli
/ Enzymes
/ Photon correlation spectroscopy
/ Protein Structure, Quaternary
/ Proteins
/ Research and Analysis Methods
