TY - JOUR
T1 - Structural characterization of the binding site in the merr metalloregulatory protein
AU - Clark, Kimber
AU - Penner-Hahn, James E.
AU - Utschig, Lisa
AU - O'halloran, Thomas V.
PY - 1993/1
Y1 - 1993/1
N2 - 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-MeiR 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.
AB - 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-MeiR 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.
KW - DNA transcription
KW - MerR
KW - Metalloregulatory protein
UR - http://www.scopus.com/inward/record.url?scp=84956110314&partnerID=8YFLogxK
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U2 - 10.7567/JJAPS.32S2.536
DO - 10.7567/JJAPS.32S2.536
M3 - Article
AN - SCOPUS:84956110314
SN - 0021-4922
VL - 32
SP - 487
EP - 489
JO - Japanese Journal of Applied Physics
JF - Japanese Journal of Applied Physics
ER -