Non-Heme Manganese Catalysts for On-Demand Production of Chlorine Dioxide in Water and Under Mild Conditions

2014 ◽  
Vol 136 (9) ◽  
pp. 3680-3686 ◽  
Author(s):  
Scott D. Hicks ◽  
Doyeon Kim ◽  
Silei Xiong ◽  
Grigori A. Medvedev ◽  
James Caruthers ◽  
...  
2021 ◽  
Vol 60 (5) ◽  
pp. 2905-2913
Author(s):  
Tayyebeh B. Champ ◽  
Jun H. Jang ◽  
Justin L. Lee ◽  
Guang Wu ◽  
Michael A. Reynolds ◽  
...  

2015 ◽  
Vol 19 (01-03) ◽  
pp. 492-499 ◽  
Author(s):  
Scott D. Hicks ◽  
Silei Xiong ◽  
Curt J. Bougher ◽  
Grigori A. Medvedev ◽  
James Caruthers ◽  
...  

A water-soluble manganese porphyrin complex was examined for the catalytic formation of chlorine dioxide from chlorite under ambient temperature at pH 5.00 and 6.90. Quantitative kinetic modeling allowed for the deduction of a mechanism that accounts for all experimental observations. Catalysis is initiated via an OAT (Oxygen Atom Transfer) reaction resulting in formation of a putative manganese(V) oxo species, which undergoes ET (Electron Transfer) with chlorite to form chlorine dioxide. As chlorine dioxide accumulates in solution, chlorite consumption slows down and ClO 2 reaches a maximum as the system reaches equilibrium. In phosphate buffer at pH 6.90, manganese(IV) oxo accumulates and its reaction with ClO 2 gives ClO 3-. However, at pH 5.00 acetate buffer proton coupled electron transfer (PCET) from chlorite to manganese(IV) oxo is fast and irreversible leading to chlorate formation only via the putative manganese(V) oxo species. These differences underscore how PCET rates affect reaction pathways and mechanism. The ClO 2 product can be collected from the aqueous reaction mixture via purging with an inert gas, allowing for the preparation of chlorine dioxide on-demand.


2021 ◽  
Author(s):  
Jesse A Jones ◽  
Ajitha S Cristie-David ◽  
Michael P Andreas ◽  
Tobias W Giessen

Protein nanocages play crucial roles in sub-cellular compartmentalization and spatial control in all domains of life and have been used as biomolecular tools for applications in biocatalysis, drug delivery, and bionanotechnology. The ability to control their assembly state under physiological conditions would further expand their practical utility. To gain such control, we introduced a peptide capable of triggering conformational change at a key structural position in the largest known encapsulin nanocompartment. We report the structure of the resulting engineered nanocage and demonstrate its ability to on-demand disassemble and reassemble under physiological conditions. We demonstrate its capacity for in vivo encapsulation of proteins of choice while also demonstrating in vitro cargo loading capabilities. Our results represent a functionally robust addition to the nanocage toolbox and a novel approach for controlling protein nanocage disassembly and reassembly under mild conditions.


2019 ◽  
Vol 133 ◽  
pp. 106-114 ◽  
Author(s):  
Zaizheng Dong ◽  
Yimin Zhu ◽  
Yuexin Han ◽  
Xiaotian Gu ◽  
Kai Jiang

2008 ◽  
Author(s):  
Jamie Chamberlin
Keyword(s):  

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