Skip to main content

Some Structural Aspects of Carbonic Anhydrase

  • Conference paper
Biophysics and Physiology of Carbon Dioxide

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

Any proposed model for the active site structure and the mechanism of action of carbonic anhydrase should take into account those experimental data which are more directly related to the metal ion environment. In particular, water proton relaxation measurements of solutions of carbonic anhydrase derivatives containing paramagnetic metal ions constitute one of the most reliable insights into the solvation of the metal itself and the possible hydrogen ion equilibria involved (Fabry et al., 1970).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  • Bazzi D, Bertini I, Luchinat C, Scozzafava A (1979) The electronic spectra of cobalt (II) bovine carbonic anhydrase. Inorg Chim Acta 36: L431–432

    Article  Google Scholar 

  • Bertini I, Canti G, Luchinat C, Scozzafava A (1978a) Characterization of cobalt ( II) bovine carbonic anhydrase and of its derivatives. J Am Chem Soc 100: 4873–4877

    Article  Google Scholar 

  • Bertini I, Borghi E, Luchinat C (1978b) Characterization of nickel (II) bovine carbonic anhydrase and its inhibitor derivatives. Bioinorg Chem 9: 495 —504

    Article  Google Scholar 

  • Bertini I, Luchinat C, Scozzafava A (1978c) Binding affinity of bicarboxylate ions for cobalt ( II) bovine carbonic anhydrase. Bioinorg Chem 9: 93–100

    Article  Google Scholar 

  • Bertini I, Canti G, Luchinat C, Scozzafava A (1979) Characterization of oxovanadium ( IV) substituted bovine carbonic anhydrase B. Inorg Chini Acta 36: 9–12

    Article  Google Scholar 

  • Fabry (Riepe) ME, Koenig SH, Shillinger WE (1970) Nuclear magnetic relaxation dispersion in protein solutions. IV. Proton relaxation at the active site of carbonic anhydrase. J Biol Chem 245: 4256–4262

    Google Scholar 

  • Karman KK, Petef M, Fridborg K, Cid-Dresdner H, Lövgren S (1977) Structure and function of carbonic anhydrases. FEBS Lett 73: 115–119

    Article  Google Scholar 

  • Pesando JM (1975) Proton magnetic resonance studies of carbonic anhydrase. II. Group controlling catalytic activity. Biochemistry 14: 681–688

    Article  Google Scholar 

  • Whitney PL, Brandt H (1976) Effects of two ionizing groups on the active site of human carbonic anhydrase B. J Biol Chem 251: 3862–386

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1980 Springer-Verlag Berlin Heidelberg

About this paper

Cite this paper

Bertini, I., Luchinat, C., Scozzafava, A. (1980). Some Structural Aspects of Carbonic Anhydrase. In: Bauer, C., Gros, G., Bartels, H. (eds) Biophysics and Physiology of Carbon Dioxide. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-67572-0_16

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-67572-0_16

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-67574-4

  • Online ISBN: 978-3-642-67572-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics