Cysteine contributions to metal binding preference for Zn/Cd in the β-domain of metallothionein

Chia Ching Chang; Wen Fa Liao; P. C. Huang

Cysteine contributions to metal binding preference for Zn/Cd in the β-domain of metallothionein

Chia Ching Chang, Wen Fa Liao, P. C. Huang

Research output: Contribution to journal › Article › peer-review

Abstract

Previous studies showed that metals in the β-domain of metallothionein (MT) are more readily exchangeable and the level of avidity is site specific. This is reflected by energy differences computed with a series of simulated structures derived from X-ray crystallography. In this study, we examined further the contribution of each of the nine cysteines in the β-domain. By semi-empirical MNDO calculations, we observed that the relative average binding strength is the strongest for Cys21 to Cd[M4] and for Cys26 to Zn[M3], except for the bridging cysteines. These results suggest that binding site preference for Zn/Cd is determined by binding strength between specific cysteines and metal ion species.

Original language	English (US)
Pages (from-to)	41-46
Number of pages	6
Journal	Protein engineering
Volume	11
Issue number	1
State	Published - Jan 1998
Externally published	Yes

Keywords

Binding energy
MNDO
Metallothionein
Quantum

ASJC Scopus subject areas

Biochemistry
Molecular Biology

Cite this

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abstract = "Previous studies showed that metals in the β-domain of metallothionein (MT) are more readily exchangeable and the level of avidity is site specific. This is reflected by energy differences computed with a series of simulated structures derived from X-ray crystallography. In this study, we examined further the contribution of each of the nine cysteines in the β-domain. By semi-empirical MNDO calculations, we observed that the relative average binding strength is the strongest for Cys21 to Cd[M4] and for Cys26 to Zn[M3], except for the bridging cysteines. These results suggest that binding site preference for Zn/Cd is determined by binding strength between specific cysteines and metal ion species.",

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N2 - Previous studies showed that metals in the β-domain of metallothionein (MT) are more readily exchangeable and the level of avidity is site specific. This is reflected by energy differences computed with a series of simulated structures derived from X-ray crystallography. In this study, we examined further the contribution of each of the nine cysteines in the β-domain. By semi-empirical MNDO calculations, we observed that the relative average binding strength is the strongest for Cys21 to Cd[M4] and for Cys26 to Zn[M3], except for the bridging cysteines. These results suggest that binding site preference for Zn/Cd is determined by binding strength between specific cysteines and metal ion species.

AB - Previous studies showed that metals in the β-domain of metallothionein (MT) are more readily exchangeable and the level of avidity is site specific. This is reflected by energy differences computed with a series of simulated structures derived from X-ray crystallography. In this study, we examined further the contribution of each of the nine cysteines in the β-domain. By semi-empirical MNDO calculations, we observed that the relative average binding strength is the strongest for Cys21 to Cd[M4] and for Cys26 to Zn[M3], except for the bridging cysteines. These results suggest that binding site preference for Zn/Cd is determined by binding strength between specific cysteines and metal ion species.

KW - Binding energy

KW - MNDO

KW - Metallothionein

KW - Quantum

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Cysteine contributions to metal binding preference for Zn/Cd in the β-domain of metallothionein

Abstract

Keywords

ASJC Scopus subject areas

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