You can also search for this author in You can also search for this author in McCall, K. A., Huang, C. & Fierke, C. A. Active-site solvent replenishment observed during human carbonic anhydrase II catalysis. Get the most important science stories of the day, free in your inbox. Elucidating the role of metal ions in carbonic anhydrase catalysis
The cumulative effect of such alterations provides mechanistic insights into the overall reduction of the enzymatic activity in the non-native metal-substituted CA IIs.The coordination geometry around the metal binding site in CA II, when no CONext, we investigated the effect of metal coordination geometry on the efficacy of substrate (COOur results provide advanced insights into the role of metal ions and the metal-protein relationship for the CA II catalytic mechanism. Kim, C. U. et al. Forsman, C., Behravan, G., Osterman, A.
Nature Communications Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) in metalloproteins. Structural and functional aspects of metal sites in biology. Lindskog, S. & Nyman, P. O. Metal-binding properties of human erythrocyte carbonic anhydrases. The successful treatment of schisis cavities with carbonic anhydrase inhibitor has been previously reported.111 Genead et al.112 treated 29 eyes of 15 XLRS patients with topical dorzolamide for 441 months and noted some positive effects on visual acuity, cystoid macular lesions, and central foveal thickness.
Coleman, J. E. Metal ion dependent binding of sulphonamide to carbonic anhydrase. Thank you for visiting nature.com. This work was initiated by the support of Samsung Science and Technology Foundation (SSTF-BA1702-04) and further supported by the National Research Foundation of Korea (NRF) grant (NRF-2019R1A2C1004274) funded by the Korea government (MSIT).Department of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of KoreaJin Kyun Kim, Cheol Lee, Seon Woo Lim, Aniruddha Adhikari, Cheol-Min Ghim & Chae Un KimDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL, 32610, USAYou can also search for this author in This is why a carbonated drink does not instantly degas when opening the container; however, it will rapidly degas in the mouth when it comes in contact with carbonic anhydrase that is contained in saliva.An anhydrase is defined as an enzyme that catalyzes the removal of a water molecule from a compound, and so it is this "reverse" reaction that gives carbonic anhydrase its name, because it removes a water molecule from carbonic acid. I. The chelating agent was then removed by buffer-exchange against 50 mM Tris-HCl pH 7.8In a 96 deep-well plate, aliquots of 50 μL of 0.1 mg mLCrystals of CA II were obtained using the hanging drop vapor diffusion methodCryo-trapping the intermediate states of Zn-CA II was previously achieved by cryocooling CA II crystals under CODiffraction data were collected at Pohang Light Source II (wavelength of 0.9793 Å, beam size of 100 μm) under nitrogen cold stream (100 K). & Jonsson, B.-H. Production of active human carbonic anhydrase ll in Khalifah, R. G., Strader, D. J., Bryant, S. H. & Gibson, S. M. Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B. Coleman, J. E. Mechanism of action of carbonic anhydrase—substrate sulfonamide and anion binding. Henderson, R. Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction. J. Biol. Liang, J. Y.
The most efficient native Zn-CA II preserves a tetrahedral coordination and fine-tunes the water network embedded within the protein scaffold (Fig. A., Christianson, D. W. & Fierke, C. A. Krebs, J. F., Ippolito, J. A., Nechay, M. R. & Alexandrova, A. N. Mysteries of metals in metalloenzymes. Comparison of solution and crystal properties of Co(II)-substituted human carbonic anhydrase II. In addition, we reveal that the metal ions have a long-range (~10 Å) electrostatic effect on restructuring the water network at the active site, affecting the product displacement and the proton transfer process. To describe equilibrium in the carbonic anhydrase reaction, Le Chatelier's principle is used. Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes.