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1. Silver Binding to Bacterial Glutaredoxins Observed by NMR

Author

Stephanie M. Bilinovich, Daniel L. Morris, Jeremy W. Prokop, Joel A. Caporoso, Alexandra Taraboletti, Nilubol Duangjumpa, Matthew J. Panzner, Leah P. Shriver, and Thomas C. Leeper

Subjects
glutaredoxin, GRX, silver ion, metal binding, NMR, Biology (General), QH301-705.5
Abstract

Glutaredoxins (GRXs) are a class of enzymes used in the reduction of protein thiols and the removal of reactive oxygen species. The CPYC active site of GRX is a plausible metal binding site, but was previously theorized not to bind metals due to its cis-proline configuration. We have shown that not only do several transition metals bind to the CPYC active site of the Brucella melitensis GRX but also report a model of a dimeric GRX in the presence of silver. This metal complex has also been characterized using enzymology, mass spectrometry, size exclusion chromatography, and molecular modeling. Metalation of GRX unwinds the end of the helix displaying the CPYC active site to accommodate dimerization in a way that is similar to iron sulfur cluster binding in related homologs and may imply that metal binding is a more common occurrence in this class of oxidoreductases than previously appreciated.

Published
2021
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2. Silver Binding to Bacterial Glutaredoxins Observed by NMR

Author

Nilubol Duangjumpa, Joel Caporoso, Matthew J. Panzner, Stephanie M. Bilinovich, Jeremy W. Prokop, Thomas C. Leeper, Alexandra Taraboletti, Leah P. Shriver, and Daniel L. Morris

Subjects
chemistry.chemical_classification, GRX, biology, Molecular model, Chemistry, Stereochemistry, Metalation, QH301-705.5, silver ion, metal binding, Active site, Metal Binding Site, glutaredoxin, NMR, Metal, Enzyme, visual_art, Glutaredoxin, biology.protein, visual_art.visual_art_medium, Iron-sulfur cluster binding, General Earth and Planetary Sciences, Biology (General), General Environmental Science
Abstract

Glutaredoxins (GRXs) are a class of enzymes used in the reduction of protein thiols and the removal of reactive oxygen species. The CPYC active site of GRX is a plausible metal binding site, but was previously theorized not to bind metals due to its cis-proline configuration. We have shown that not only do several transition metals bind to the CPYC active site of the Brucella melitensis GRX but also report a model of a dimeric GRX in the presence of silver. This metal complex has also been characterized using enzymology, mass spectrometry, size exclusion chromatography, and molecular modeling. Metalation of GRX unwinds the end of the helix displaying the CPYC active site to accommodate dimerization in a way that is similar to iron sulfur cluster binding in related homologs and may imply that metal binding is a more common occurrence in this class of oxidoreductases than previously appreciated.

Published
2021

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