Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 May;74(5):1794–1797. doi: 10.1073/pnas.74.5.1794

X-ray absorption studies of halide binding to carbonic anhydrase.

G S Brown, G Navon, R G Shulman
PMCID: PMC431002  PMID: 405667

Abstract

X-ray absorption measurements of bovine carbonic anhydrase B have been made at the the Stanford Synchrotron Radiation Project with a spectrometer operating in the fluorescence mode. Differences in absorption at and beyond the zinc K-edge near 9664 ev have been observed upon the addition of bromide or iodide. The additional absorption in k space, out to k approximately 7 A-1, obtained upon the addition of iodide has been compared with the absorption in this region of a ZnI2 sample. The similarities between these absorptions lead to the conclusion that the zinc-iodide distance in the protein is 2.65 +/-0.06 A; it is known to be 2.62 A in ZnI2. This shows that the iodide binds directly to the zinc in the protein.

Full text

PDF
1794

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Grell E., Bray R. C. Electron paramagnetic resonance spectroscopy of bovine cobalt carbonic anhydrase B. Biochim Biophys Acta. 1971 May 25;236(2):503–506. doi: 10.1016/0005-2795(71)90232-7. [DOI] [PubMed] [Google Scholar]
  2. KERNOHAN J. C. THE PH-ACTIVITY CURVE OF BOVINE CARBONIC ANHYDRASE AND ITS RELATIONSHIP TO THE INHIBITION OF THE ENZYME BY ANIONS. Biochim Biophys Acta. 1965 Feb 22;96:304–317. [PubMed] [Google Scholar]
  3. Kannan K. K., Liljas A., Waara I., Bergstén P. C., Lövgren S., Strandberg B., Bengtsson U., Carlbom U., Fridborg K., Järup L. Crystal structure of human erythrocyte carbonic anhydrase C. VI. The three-dimensional structure at high resolution in relation to other mammalian carbonic anhydrases. Cold Spring Harb Symp Quant Biol. 1972;36:221–231. doi: 10.1101/sqb.1972.036.01.030. [DOI] [PubMed] [Google Scholar]
  4. Kincaid B. M., Eisenberger P., Hodgson K. O., Doniach S. X-ray absorption spectroscopy using synchrotron radiation for structural investigation of organometallic molecules of biological interest. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2340–2342. doi: 10.1073/pnas.72.6.2340. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Koenig S. H., Brown R. D., 3rd Inhibition by anions of human red cell carbonic anhydrase B: physiological and biochemical implications. Science. 1976 Nov 12;194(4266):745–747. doi: 10.1126/science.10627. [DOI] [PubMed] [Google Scholar]
  6. LINDSKOG S. Effects of pH and inhibitors on some properties related to metal binding in bovine carbonic anhydrase. J Biol Chem. 1963 Mar;238:945–951. [PubMed] [Google Scholar]
  7. LINDSKOG S. Purification and properties of bovine erythrocyte carbonic anhydrase. Biochim Biophys Acta. 1960 Apr 8;39:218–226. doi: 10.1016/0006-3002(60)90156-6. [DOI] [PubMed] [Google Scholar]
  8. Lanir A., Navon G. Interaction of bovine carbonic anhydrase with acetate ions. Biochim Biophys Acta. 1974 Mar 21;341(1):65–74. doi: 10.1016/0005-2744(74)90066-7. [DOI] [PubMed] [Google Scholar]
  9. Lanir A., Navon G. NMR studies of the two binding sites of acetate ions to manganese(II) carbonic anhydrase. Biochim Biophys Acta. 1974 Mar 21;341(1):75–84. doi: 10.1016/0005-2744(74)90067-9. [DOI] [PubMed] [Google Scholar]
  10. Lindskog S. Interaction of cobalt(II)--carbonic anhydrase with anions. Biochemistry. 1966 Aug;5(8):2641–2646. doi: 10.1021/bi00872a023. [DOI] [PubMed] [Google Scholar]
  11. Maren T. H. Carbonic anhydrase: chemistry, physiology, and inhibition. Physiol Rev. 1967 Oct;47(4):595–781. doi: 10.1152/physrev.1967.47.4.595. [DOI] [PubMed] [Google Scholar]
  12. Maren T. H. Inhibition by anions of human red cell carbonic anhydrase B: physiological and biochemical implications. Science. 1976 Nov 12;194(4266):746–747. doi: 10.1126/science.194.4266.746. [DOI] [PubMed] [Google Scholar]
  13. Maren T. H., Rayburn C. S., Liddell N. E. Inhibition by anions of human red cell carbonic anhydrase B: physiological and biochemical implications. Science. 1976 Feb 6;191(4226):469–472. doi: 10.1126/science.813299. [DOI] [PubMed] [Google Scholar]
  14. Pocker Y., Stone J. T. The catalytic versatility of erythrocyte carbonic anhydrase. VI. Kinetic studies of noncompetitive inhibition of enzyme-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry. 1968 Aug;7(8):2936–2945. doi: 10.1021/bi00848a034. [DOI] [PubMed] [Google Scholar]
  15. Roughton F. J., Booth V. H. The effect of substrate concentration, pH and other factors upon the activity of carbonic anhydrase. Biochem J. 1946;40(2):319–330. doi: 10.1042/bj0400319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Shulman G. R., Yafet Y., Eisenberger P., Blumberg W. E. Observations and interpretation of x-ray absorption edges in iron compounds and proteins. Proc Natl Acad Sci U S A. 1976 May;73(5):1384–1388. doi: 10.1073/pnas.73.5.1384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Shulman R. G., Eisenberger P., Blumberg W. E., Stombaugh N. A. Determination of the iron-sulfur distances in rubredoxin by x-ray absorption spectroscopy. Proc Natl Acad Sci U S A. 1975 Oct;72(10):4003–4007. doi: 10.1073/pnas.72.10.4003. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Taylor J. S., Coleman J. E. Electron spin resonance of metallocarbonic anhydrases. J Biol Chem. 1971 Nov 25;246(22):7058–7067. [PubMed] [Google Scholar]
  19. Ward R. L. 35C1 nuclear magnetic resonance studies of a zinc metalloenzyme carbonic anhydrase. Biochemistry. 1969 May;8(5):1879–1883. doi: 10.1021/bi00833a016. [DOI] [PubMed] [Google Scholar]
  20. Ward R. L., Cull M. D. Temperature and competitive anion-binding studies of carbonic anhydrase. Arch Biochem Biophys. 1972 Jun;150(2):436–439. doi: 10.1016/0003-9861(72)90060-4. [DOI] [PubMed] [Google Scholar]
  21. Ward R. L., Whitney P. L. 81 Br-NMR studies of carbonic anhydrase. Biochem Biophys Res Commun. 1973 Mar 17;51(2):343–348. doi: 10.1016/0006-291x(73)91263-1. [DOI] [PubMed] [Google Scholar]
  22. Ward R. L. Zinc environmental differences in carbonic anhydrase isozymes. Biochemistry. 1970 Jun 9;9(12):2447–2454. doi: 10.1021/bi00814a009. [DOI] [PubMed] [Google Scholar]
  23. Yeagle P. L., Lochmüller C. H., Henkens R. W. 13-C nuclear magnetic resonance studies on the mechanism of action of carbonic anhydrase. Proc Natl Acad Sci U S A. 1975 Feb;72(2):454–458. doi: 10.1073/pnas.72.2.454. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Zeppezauer M., Lindman B., Forsén S., Lindqvist I. A 81Br nuclear magnetic resonance study of bromide ion binding to proteins in aqueous solution. Biochem Biophys Res Commun. 1969 Sep 24;37(1):137–142. doi: 10.1016/0006-291x(69)90891-2. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES