STRUCTURAL CHARACTERIZATION OF THE BINDING-SITE IN THE MERR METALLOREGULATORY PROTEIN

被引：1

作者：

CLARK, K ^{[1
]}

UTSCHIG, L ^{[1
]}

OHALLORAN, TV ^{[1
]}

PENNERHAHN, JE ^{[1
]}

机构：

[1] NORTHWESTERN UNIV, DEPT CHEM, EVANSTON, IL 60208 USA

来源：

JAPANESE JOURNAL OF APPLIED PHYSICS PART 1-REGULAR PAPERS BRIEF COMMUNICATIONS & REVIEW PAPERS | 1993年 / 32卷

关键词：

DNA TRANSCRIPTION; METALLOREGULATORY PROTEIN; MERR;

D O I：

10.7567/JJAPS.32S2.536

中图分类号：

O59 [应用物理学];

学科分类号：

摘要：

The Zinc and Cadmium forms of MerR, a metalloregulatory protein involved in bacterial mercury detoxification have been studied using X-ray absorption spectroscopy. Previous work has shown the Hg-MerR to have a unique three coordinate HgS3 environment. Preliminary analysis of the EXAFS data for the Cd- and Zn-MerR derivatives suggests a higher coordination number in these cases.

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页码：536 / 537

页数：2

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