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Elucidating the role of metal ions in carbonic anhydrase catalysis.


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.

SUBMITTER: Kim JK 

PROVIDER: S-EPMC7486293 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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Elucidating the role of metal ions in carbonic anhydrase catalysis.

Kim Jin Kyun JK   Lee Cheol C   Lim Seon Woo SW   Adhikari Aniruddha A   Andring Jacob T JT   McKenna Robert R   Ghim Cheol-Min CM   Kim Chae Un CU  

Nature communications 20200911 1


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 (te  ...[more]

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