ReviewBiochimica et biophysica acta2010
Proton transport in carbonic anhydrase: Insights from molecular simulation.
Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed.
- Conformational flexibility of His200 enables catalytic activity in the T200H mutant of carbonic anhydrase II.Molecules and cells · 2025Article
- Carbonic Anhydrase Robustness for Use in Nanoscale COACS omega · 2023Article
- The Crystal Structure of a hCA VII Variant Provides Insights into the Molecular Determinants Responsible for Its Catalytic Behavior.International journal of molecular sciences · 2018Article
- Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II.The journal of physical chemistry. B · 2016Article
- Modeling the structure and proton transfer pathways of the mutant His-107-Tyr of human carbonic anhydrase II.Journal of molecular modeling · 2013Article
- Dynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent.The Journal of biological chemistry · 2012Article
- Intrinsic proton-donating power of zinc-bound water in a carbonic anhydrase active site model estimated by NMR.Journal of the American Chemical Society · 2011Article
- Kinetic and crystallographic studies of the role of tyrosine 7 in the active site of human carbonic anhydrase II.Archives of biochemistry and biophysics · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
This article reviews the insights gained from molecular simulations of human carbonic anhydrase II (HCA II) utilizing non-reactive and reactive force fields. The simulations with a reactive force field explore protein transfer and transport via Grotthuss shuttling, while the non-reactive simulations probe the larger conformational dynamics that underpin the various contributions to the rate-limiting proton transfer event. Specific attention is given to the orientational stability of the His64 group and the characteristics of the active site water cluster, in an effort to determine both of their impact on the maximal catalytic rate. The explicit proton transfer and transport events are described by the multistate empirical valence bond (MS-EVB) method, as are alternative pathways for the excess proton charge defect to enter/leave the active site. The simulation results are interpreted in light of experimental results on the wild-type enzyme and various site-specific mutations of HCA II in order to better elucidate the key factors that contribute to its exceptional efficiency.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.