Chromate Binding and Removal by the Molybdate-Binding Protein ModA.
Effective and cheap methods and techniques for the safe removal of hexavalent chromate from the environment are in increasingly high demand. High concentrations of hexavalent chromate have been shown to have numerous harmful effects on human biology. We show that the E. coli molybdate-binding protein ModA is a genetically encoded tool capable of removing chromate from aqueous solutions. Although previously reported to not bind chromate, we show that ModA binds chromate tightly and is capable of removing chromate to levels well below current US federal standards.
Department of Chemistry, University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Jason
J
Karpus
Department of Chemistry, University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Michael
M
Bosscher
Department of Chemistry, University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Ifedayo
I
Ajiboye
Department of Chemistry, University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Liang
L
Zhang
Department of Chemistry, University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Chuan
C
He
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry; D001665:Binding Sites; D002614:Chelating Agents / Q000737:chemistry*; D002840:Chromates / Q000737:chemistry*; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry*; D005453:Fluorescence; D005470:Fluorometry; D033902:Periplasmic Binding Proteins / Q000737:chemistry*; D011485:Protein Binding; D055550:Protein Stability
D001425:Bacterial Outer Membrane Proteins; D002614:Chelating Agents; D002840:Chromates; D029968:Escherichia coli Proteins; C098002:ModA protein, E coli; D033902:Periplasmic Binding Proteins; C078167:OMPA outer membrane proteins
bioinorganic chemistry; environmental chemistry; fluorescence spectroscopy; hexavalent chromium; metalloproteins