An Extremely Stable Interprotein Tetrahedral Hg(Cys)₄ Core Forms in the Zinc Hook Domain of Rad50 Protein at Physiological pH.

ABSTRACT: In nature, thiolate-based systems are the primary targets of divalent mercury (Hg^II ) toxicity. The formation of Hg(Cys)_x cores in catalytic and structural protein centers mediates mercury's toxic effects and ultimately leads to cellular damage. Multiple studies have revealed distinct Hg^II -thiolate coordination preferences, among which linear Hg^II complexes are the most commonly observed in solution at physiological pH. Trigonal or tetrahedral geometries are formed at basic pH or in tight intraprotein Cys-rich metal sites. So far, no interprotein tetrahedral Hg^II complex formed at neutral pH has been reported. Rad50 protein is a part of the multiprotein MRN complex, a major player in DNA damage-repair processes. Its central region con

SUBMITTER: Luczkowski M 

PROVIDER: S-EPMC9828754 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature