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Physiological levels of glutathione enhance Zn(II) binding by a Cys4 zinc finger.

Abstract：

:Using fluorescence and UV-vis spectroscopies and mass spectrometry, we demonstrated that the presence of physiological levels of reduced glutathione enhances the binding of Zn(II) to XPAzf, a Cys4 zinc finger peptide derived from the XPA protein, by means of formation of a ternary complex of a general formula ZnXPAzf[GSH]. Similar complexes were also indicated by ESI-MS for isostructural Co(II)- and Cd(II)-substituted XPAzf. The observed enhancement of the Zn(II) binding to XPAzf by a factor of 50 over the physiological range of GSH concentrations of 1-20 mM corresponds to a dissociation constant of GSH from the ZnXPAzf[GSH] complex of 0.05 microM. This effect may account for an apparent discrepancy between relatively low Zn(II) binding constants measured in vitro for many zinc fingers, and the requirement of tight Zn(II) binding enforced by intracellular zinc buffering by the thionein/metallothionein couple.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Piatek K,Hartwig A,Bal W

doi

10.1016/j.bbrc.2009.08.128

subject

Has Abstract

pub_date

2009-11-13 00:00:00

pages

265-8

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)01721-5

journal_volume

389

pub_type

杂志文章

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