Modeling Post-Translational Modification in Cobalt Nitrile Hydratase with a Metallopeptide from Anne Jones

Authors

Arpita Saha, Georgia Southern UniversityFollow
Gerard Rowe, University of South Carolina - AikenFollow
Lei Yang, University of Central ArkansasFollow
Nancy Williams, Claremont McKenna CollegeFollow
Robert Holbrook, Northwestern UniversityFollow
Sibrina Collins, Lawrence Technological UniversityFollow
Karin Young, Centre CollegeFollow

Document Type

Article

Publication Date

7-17-2014

Publication Title

Virtual Inorganic Pedagogical Electronic Resource

Abstract

In this literature discussion, students read a paper about a cobalt metallopeptide that imitates the active site of the enzyme nitrile hydratase. Specifically, the model complex is oxidized by air to produce a coordination sphere with both cysteine thiolate and sulfinic acid ligands, much like the post-translationally oxidized cysteine ligands in the biological system. This paper also provides an introduction to a variety of physical methods used to characterize the structure, including X-ray absorbance spectroscopy, magnetic susceptibility using the Evans method, IR spectroscopy, electronic absorbance spectroscopy, and electron paramagnetic resonance spectroscopy. This LO was created for the 2014 TUES Viper Workshop on bioinorganic chemistry.

Recommended Citation

Saha, Arpita, Gerard Rowe, Lei Yang, Nancy Williams, Robert Holbrook, Sibrina Collins, Karin Young. 2014. "Modeling Post-Translational Modification in Cobalt Nitrile Hydratase with a Metallopeptide from Anne Jones." Virtual Inorganic Pedagogical Electronic Resource: The American Chemical Society and Division of Chemical Education, Inc. source: ionicviper.org
https://digitalcommons.georgiasouthern.edu/chem-facpubs/145