English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Krypton-derivatization highlights O-2-channeling in a four-electron reducing oxidase

MPS-Authors
/persons/resource/persons256582

Wagner,  Tristan
Research Group Microbial Metabolism, Max Planck Institute for Marine Microbiology, Max Planck Society;

External Resource
No external resources are shared
Fulltext (public)

Wagner20.pdf
(Publisher version), 3MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Engilberge, S., Wagner, T., Carpentier, P., Girard, E., & Shima, S. (2020). Krypton-derivatization highlights O-2-channeling in a four-electron reducing oxidase. Chemical Communications, 56(74), 10863-10866. doi:10.1039/d0cc04557h.


Cite as: http://hdl.handle.net/21.11116/0000-0007-F1D8-5
Abstract
F420H2-oxidase (FprA) catalyses the four-electron reduction of O(2)to 2H(2)O using the reduced form of F(420)as electron donor. The hydrophobic O-2-channel detected by Kr-derivatization and the concerted movement of a gating loop could contribute to prevent unwanted side-reaction between the catalytic intermediates and solvents, therefore preventing reactive oxygen species formation.