English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Structures of the sulfite detoxifying F-420-dependent enzyme from Methanococcales

MPS-Authors
/persons/resource/persons256580

Jespersen,  Marion
Research Group Microbial Metabolism, Max Planck Institute for Marine Microbiology, Max Planck Society;

/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 (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

s41589-022-01232-y.pdf
(Publisher version), 13MB

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

Jespersen, M., Pierik, A. J., & Wagner, T. (2023). Structures of the sulfite detoxifying F-420-dependent enzyme from Methanococcales. NATURE CHEMICAL BIOLOGY. doi:10.1038/s41589-022-01232-y.


Cite as: https://hdl.handle.net/21.11116/0000-000D-42BD-4
Abstract
Methanogenic archaea are main actors in the carbon cycle but are sensitive to reactive sulfite. Some methanogens use a sulfite detoxification system that combines an F420H2-oxidase with a sulfite reductase, both of which are proposed precursors of modern enzymes. Here, we present snapshots of this coupled system, named coenzyme F-420-dependent sulfite reductase (Group I Fsr), obtained from two marine methanogens. Fsr organizes as a homotetramer, harboring an intertwined six-[4Fe-4S] cluster relay characterized by spectroscopy. The wire, spanning 5.4 nm, electronically connects the flavin to the siroheme center. Despite a structural architecture similar to dissimilatory sulfite reductases, Fsr shows a siroheme coordination and a reaction mechanism identical to assimilatory sulfite reductases. Accordingly, the reaction of Fsr is unidirectional, reducing sulfite or nitrite with F420H2. Our results provide structural insights into this unique fusion, in which a primitive sulfite reductase turns a poison into an elementary block of life.