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Updated: Dec 22, 2025

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
Published on: January 17, 2020
Surprising cofactors in metalloenzymes
Catherine L Drennan1, John W Peters
1Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA. cdrennan@mit.edu
Abstract:
Transition metal complexes are located at the active sites of a number of enzymes involved in intriguing biochemical reactions. These complexes can exhibit a wide variety of chemical reactivity due to the ease at which transition metals can adopt different coordination environments and oxidation states. Crystallography has been a powerful technique for examining the structure and conformational variability of complex biological metallocenters. In particular, the past ten years have provided a wealth of structural information and several surprises concerning the metallocenters at the active sites of nitrogenase, hydrogenase and carbon monoxide dehydrogenase/acetyl-coenzyme A synthase.
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