Evaluating the involvement of tryptophan on thiolated peptide-mercury(II) complexes: Cation-pi interactions-Reference-Cited by-同舟云学术

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Evaluating the involvement of tryptophan on thiolated peptide-mercury(II) complexes: Cation-pi interactions

Published:2020-06 Issue: Volume:506 Page:119552
ISSN:0020-1693
Container-title:Inorganica Chimica Acta
language:en
Short-container-title:Inorganica Chimica Acta

Author:

Ngu-Schwemlein Maria,Merle John,Meeker William,Risdon-Langdon Kierah,Nixon Timothy

Funder

National Science Foundation

Publisher

Elsevier BV

Subject

Materials Chemistry,Inorganic Chemistry,Physical and Theoretical Chemistry

Reference54 articles.

1. Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system;Steele;Biochemistry,1997

2. X-ray structure of a Hg2+ complex of mercuric reductase (MerA) and quantum mechanical/molecular mechanical study of Hg2+ transfer between the C-terminal and buried catalytic site cysteine pairs;Lian;Biochemistry,2014

3. Bacterial resistance to mercury — reductio ad absurdum?;Brown;Trends Biochem. Sci.,1985

4. Copper transport systems are involved in multidrug resistance and drug transport;Tatsuhiko;Curr. Med. Chem.,2008

5. Impact of cofactor on stability of bacterial (CopZ) and human (Atox1) copper chaperones;Hussain;Biochim. Biophys. Acta, Proteins Proteomics,2007

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4. Extracellular polymeric substances enhance dissolution and microbial methylation of mercury sulfide minerals;Environmental Science: Processes & Impacts;2023

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