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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Chemistry (Weinheim an der Bergstrasse, Germany)

Mercury(II) Binding to Metallothionein in Mytilus edulis revealed by High Energy-Resolution XANES Spectroscopy

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Chemistry (Weinheim an der Bergstrasse, Germany) - 27 Dec 2018

Manceau A, Bustamante P, Haouz A, Bourdineaud JP, Gonzalez-Rey M, Lemouchi C, Gautier-Luneau I, Geertsen V, Barruet E, Rovezzi M, Glatzel P, Pin S

Link to Pubmed [PMID] – 30426580

Chemistry 2019 Jan;25(4):997-1009

Of all divalent metals, mercury (Hg ) has the highest affinity for metallothioneins. Hg is considered to be enclosed in the α and β domains as tetrahedral α-type Hg Cys and β-type Hg Cys clusters similar to Cd and Zn . However, neither the four-fold coordination of Hg nor the existence of Hg-Hg atomic pairs have ever been demonstrated, and the Hg partitioning among the two protein domains is unknown. Using high energy-resolution XANES spectroscopy, MP2 geometry optimization, and biochemical analysis, evidence for the coexistence of two-coordinate Hg-thiolate complex and four-coordinate Hg-thiolate cluster with a metacinnabar-type (β-HgS) structure in the α domain of separate metallothionein molecules from blue mussel under in vivo exposure is provided. The findings suggest that the CXXC claw setting of thiolate donors, which only exists in the α domain, acts as a nucleation center for the polynuclear complex and that the five CXC motifs from this domain serve as the cluster-forming motifs. Oligomerization is driven by metallophilic Hg⋅⋅⋅Hg interactions. Our results provide clues as to why Hg has higher affinity for the α than the β domain. More generally, this work provides a foundation for understanding how metallothioneins mediate mercury detoxification in the cell under in vivo conditions.

https://www.ncbi.nlm.nih.gov/pubmed/30426580