DOI: 10.1111/j.1432-1033.1982.tb06494.x. The Interaction of Sulfate with Carbonic Anhydrase

The Interaction of Sulfate with Carbonic Anhydrase

10.1111/j.1432-1033.1982.tb06494.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

In the absence of sulfate the pH/rate profile for the 4‐nitrophenyl acetate hydrolase activity of bovine carbonic anhydrase is complex. The results fit with a microscopic ionization scheme involving two electrostatically interacting groups. The activity depends on the concentration of the basic form of one of these groups. Proton NMR spectra show that the active site residue, His‐64, has titration behaviour corresponding to that of the second group of the ionization scheme. The addition of increasing concentrations of Na2SO4 gradually converts the pH/rate profile to that of a simple titration curve. A pKa of 6.9 is found at 50 mM Na2SO4. Concomitantly the titration curve of His‐64 changes. The results fit with the microscopic ionization scheme if it is assumed that significant SO2−4binding occurs only when both His‐64 and the activity‐linked group are protonated. At constant pH, sulfate behaves as if it inhibits the enzyme only partially. However, data are presented suggesting that the enzyme‐sulfate complex is inactive, but the binding of SO2−4depends strongly on ionic strength. Thus, above about 25 mM sulfate any further increase of the sulfate concentration is nearly compensated by a decrease of the binding affinity. The binding of a monovalent anion, C1−, also depends on ionic strength, but this dependence is much less prominent than for SO2‐4. Sulfate shows non‐competitive behaviour with respect to CO2 and appears to compete with HCO−3. Iodide and sulfate appear to be mutually competitive. The low pH limit of Ki for I−is 3 mM and about 0.1 mM in the presence of 50 mM Na2SO4 and in the absence of sulfate respectively. In the absence of sulfate the Co(II)‐substituted bovine enzyme shows a complex pH/rate profile similar to that of the native enzyme. Changes of the optical spectrum parallel those of the activity. Relaxation rates (T−11)of water protons in the presence of Co(II) enzyme indicate that the Co(II)ion might have a H2O ligand at low pH in sulfate‐free solutions. The effects on sulfate of human carbonic anhydrase II (or C) are similar to those on the bovine enzyme. The effects of sulfate on the human 1 (or B) enzyme are smaller.

Bibliography

SIMONSSON, I., & LINDSKOG, S. (1982). The Interaction of Sulfate with Carbonic Anhydrase. European Journal of Biochemistry, 123(1), 29â36. Portico.

Authors 2

Ingvar SIMONSSON (first)
Sven LINDSKOG (additional)

References 35 Referenced 71

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Dates

Type	When
Created	20 years, 6 months ago (March 3, 2005, 4:52 p.m.)
Deposited	1 year, 9 months ago (Nov. 23, 2023, 1:59 p.m.)
Indexed	1 month, 1 week ago (July 24, 2025, 7:27 a.m.)
Issued	43 years, 6 months ago (March 1, 1982)
Published	43 years, 6 months ago (March 1, 1982)
Published Online	20 years, 6 months ago (March 3, 2005)
Published Print	43 years, 6 months ago (March 1, 1982)

Funders 0

None

BibTeX

@article{SIMONSSON_1982, title={The Interaction of Sulfate with Carbonic Anhydrase}, volume={123}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1982.tb06494.x}, DOI={10.1111/j.1432-1033.1982.tb06494.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={SIMONSSON, Ingvar and LINDSKOG, Sven}, year={1982}, month=mar, pages={29–36} }

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