Elucidating the role of metal ions in carbonic anhydrase catalysis

Jin Kyun Kim, Cheol Lee, Seon Woo Lim, Aniruddha Adhikari, Jacob T. Andring, Robert McKenna, Cheol-Min Ghim and Chae Un Kim ()
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Jin Kyun Kim: Department of Physics, Ulsan National Institute of Science and Technology (UNIST)
Cheol Lee: Department of Physics, Ulsan National Institute of Science and Technology (UNIST)
Seon Woo Lim: Department of Physics, Ulsan National Institute of Science and Technology (UNIST)
Aniruddha Adhikari: Department of Physics, Ulsan National Institute of Science and Technology (UNIST)
Jacob T. Andring: Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida
Robert McKenna: Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida
Cheol-Min Ghim: Department of Physics, Ulsan National Institute of Science and Technology (UNIST)
Chae Un Kim: Department of Physics, Ulsan National Institute of Science and Technology (UNIST)

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: 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 Zn2+, tetrahedral to octahedral conversion for Co2+, octahedral for Ni2+, and trigonal bipyramidal for Cu2+) 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.

Date: 2020
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DOI: 10.1038/s41467-020-18425-5

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