Journal
CHEMICAL SCIENCE
Volume 11, Issue 5, Pages 1241-1247Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9sc05900h
Keywords
-
Categories
Funding
- National Institutes of Health [1R35GM126961]
Ask authors/readers for more resources
The active site of [FeFe] hydrogenase, the H-cluster, consists of a canonical [4Fe-4S](H) subcluster linked to a unique binuclear [2Fe](H) subcluster containing three CO, two CN- and a bridging azadithiolate (adt, NH(CH2S-)(2)) ligand. While it is known that all five diatomic ligands are derived from tyrosine, there has been little knowledge as to the formation and installation of the adt ligand. Here, by using a combination of a cell-free in vitro maturation approach with pulse electronic paramagnetic resonance spectroscopy, we discover that serine donates the nitrogen atom and the CH2 group to the assembly of the adt ligand. More specifically, both CH2 groups in adt are sourced from the C3 methylene of serine.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available