AI Article Synopsis
- The research investigates how different metal ions influence the activity of the human metalloenzyme carbonic anhydrase II (CA II), focusing on both native zinc and non-native metal substitutions.
- Different metal ions result in varying coordination geometries (like tetrahedral for Zn and octahedral for Ni) that significantly affect the enzyme's catalytic efficiency.
- The study also highlights that metal ions can impact the enzyme's function by altering the water network in its active site, demonstrating their importance in the catalytic mechanism beyond just their chemical properties.
Article Abstract
Why metalloenzymes often show dramatic changes in their catalytic activity when subjected to chemically similar but non-native metal substitutions is a long-standing puzzle. Here, we report on the catalytic roles of metal ions in a model metalloenzyme system, human carbonic anhydrase II (CA II). Through a comparative study on the intermediate states of the zinc-bound native CA II and non-native metal-substituted CA IIs, we demonstrate that the characteristic metal ion coordination geometries (tetrahedral for Zn, tetrahedral to octahedral conversion for Co, octahedral for Ni, and trigonal bipyramidal for Cu) directly modulate the catalytic efficacy. In addition, we reveal that the metal ions have a long-range (~10 Å) electrostatic effect on restructuring water network in the active site. Our study provides evidence that the metal ions in metalloenzymes have a crucial impact on the catalytic mechanism beyond their primary chemical properties.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7486293 | PMC |
| http://dx.doi.org/10.1038/s41467-020-18425-5 | DOI Listing |
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