Neutron crystallographic studies of carbonic anhydrase

Jacob E Combs; Jacob T Andring; Robert McKenna

doi:10.1016/bs.mie.2020.01.003

Neutron crystallographic studies of carbonic anhydrase

Methods Enzymol. 2020:634:281-309. doi: 10.1016/bs.mie.2020.01.003. Epub 2020 Feb 10.

Authors

Jacob E Combs¹, Jacob T Andring¹, Robert McKenna²

Affiliations

¹ Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL, United States.
² Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL, United States. Electronic address: rmckenna@ufl.edu.

PMID: 32093837
DOI: 10.1016/bs.mie.2020.01.003

Abstract

The carbonic anhydrases (CAs; EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible hydration of carbon dioxide (CO₂) and bicarbonate (HCO₃^-). Since their discovery in 1933, CAs have been at the forefront of scientific discovery: the understanding of enzymatic reactions, structural biology, molecular dynamics, drug discovery, and clinical medicine. These ubiquitous enzymes equilibrate the reaction between CO₂, HCO₃^-, and protons. Hence, CAs have important roles in ion transport, acid-base regulation, gas exchange, photosynthesis, and CO₂ fixation. In this chapter, we describe the protocols leading to, and the analysis of CA neutron crystal structures. This accumulation of structural knowledge adds to our understanding of the enzymatic mechanism and development of CA inhibitors.

Keywords: CO(2); Carbonic anhydrase; Carbonic anhydrase II; Carbonic anhydrase IX; HCO(3)(–); Neutron crystallography; Protein; X-ray crystallography.

MeSH terms

Bicarbonates
Carbon Dioxide
Carbonic Anhydrase Inhibitors
Carbonic Anhydrases*
Neutrons

Substances

Bicarbonates
Carbonic Anhydrase Inhibitors
Carbon Dioxide
Carbonic Anhydrases