Coordination Dynamics of Zinc Triggers the Rate Determining Proton Transfer in Human Carbonic Anhydrase II.
Carbonic anhydrase
coordination dynamics
proton transfer
transition path sampling
zinc
Journal
Chemphyschem : a European journal of chemical physics and physical chemistry
ISSN: 1439-7641
Titre abrégé: Chemphyschem
Pays: Germany
ID NLM: 100954211
Informations de publication
Date de publication:
02 07 2020
02 07 2020
Historique:
received:
04
03
2020
revised:
17
04
2020
pubmed:
25
4
2020
medline:
26
1
2021
entrez:
25
4
2020
Statut:
ppublish
Résumé
We present, for the first time, how transient changes in the coordination number of zinc ion affects the rate determining step in the enzyme human carbonic anhydrase (HCA) II. The latter involves an intramolecular proton transfer between a zinc-bound water and a distant histidine residue (His-64). In the absence of time-resolved experiments, results from classical and QM-MM molecular dynamics and transition path sampling simulations are presented. The catalytic zinc ion is found to be present in two possible coordination states; viz. a stable tetra-coordinated state, T and a less stable penta-coordinated state, P with tetrahedral and trigonal bipyramidal coordination geometries, respectively. A fast dynamical inter-conversion occurs between T and P due to reorganization of active site water molecules making the zinc ion more positively charged in state P. When initiated from different coordination environments, the most probable mechanism of proton transfer is found to be deprotonation of the equatorial water molecule from state P and transfer of the excess proton via a short path formed by hydrogen bonded network of active site water molecules. We estimate the rate constant of proton transfer as
Identifiants
pubmed: 32329944
doi: 10.1002/cphc.202000177
doi:
Substances chimiques
Coordination Complexes
0
Protons
0
Water
059QF0KO0R
Histidine
4QD397987E
Carbonic Anhydrase II
EC 4.2.1.-
CA2 protein, human
EC 4.2.1.1
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1455-1473Subventions
Organisme : Science and Engineering Research Board
ID : SR/FST/CSII-011/2005
Pays : International
Organisme : UGC-DAE Consortium for Scientific Research, University Grants Commission
Pays : International
Informations de copyright
© 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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