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Juneina Omeiri

As seen in: Nature, Wiley Online Library
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Articles

Maturation of the [FeFe]‐Hydrogenase: Direct Transfer of the (κ3‐cysteinate)FeII(CN)(CO)2 Complex B from HydG to HydE

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By Juneina Omeiri, Univ. Grenoble-Alpes, Lydie Martin, Cnrs Ibs
| Wiley Online Library Verified
[FeFe]-Hydrogenases are enzymes capable of catalyzing reversible hydrogen oxidation with very high efficacy.1 Their active site is deeply buried in the protein matrix and corresponds to an organometallic compound termed H-cluster, which can be best described as a [Fe4S4] cluster connected to a diiron subcluster [2Fe]H.2 The latter is composed of two iron atoms, each bound to one carbon monoxide and one cyanide ligand.
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Structure of the human heparan sulfate polymerase complex EXT1-EXT2 - Nature Communications

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By Francisco Leisico, Juneina Omeiri, Michael Hons, Guy Schoehn, Yohann COUTE, David Bonnaffé, Hugues Lortat-Jacob
| Nature Verified
Abstract Heparan sulfates are complex polysaccharides that mediate the interaction with a broad range of protein ligands at the cell surface. A key step in heparan sulfate biosynthesis is catalyzed by the bi-functional glycosyltransferases EXT1 and EXT2, which generate the glycan backbone consisting of repeating N-acetylglucosamine and glucuronic acid units. The molecular mechanism of heparan sulfate chain polymerization remains, however, unknown.
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