6LUW

Elucidating the role of metal ions in carbonic anhydrase catalysis.

(2020) Nat Commun 11: 4557-4557

• PubMed: 32917908 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/s41467-020-18425-5
• Primary Citation of Related Structures:  
  6LUU, 6LUV, 6LUW, 6LUX, 6LUY, 6LUZ, 6LV1, 6LV2, 6LV3, 6LV4, 6LV5, 6LV6, 6LV7, 6LV8, 6LV9, 6LVA


• PubMed 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 ²⁺ , tetrahedral to octahedral conversion for Co ²⁺ , octahedral for Ni ²⁺ , and trigonal bipyramidal for Cu ²⁺ ) directly modulate the catalytic efficacy. In addition, we reveal that the metal ions have a long-range (~10??) 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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Organizational Affiliation: 

Department of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.