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Effects of pH and inhibitors on the absorption spectrum of cobalt(II)‐substituted carbonic anhydrase III from bovine skeletal muscle
Author(s) -
Engberg Paul,
Lindskog Sven
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81337-x
Subject(s) - carbonic anhydrase , cobalt , chemistry , absorption (acoustics) , biochemistry , absorption spectroscopy , inorganic chemistry , enzyme , materials science , physics , quantum mechanics , composite material
Bovine apocarbonic anhydrase III has been prepared by incubation with 2‐carboxy‐1,10‐phenanthroline at pH 5.5. The Co(II)‐substituted enzyme has been prepared and its absorption spectrum has been studied. The spectrum is nearly pH‐independent above pH 6. It is very similar to the high pH spectral forms of Co(II)‐carbonic anhydrases I and II. The spectra of complexes with the sulfonamide inhibitor, acetazolamide, and with CN − and NCO − are virtually identical to the spectra of the corresponding complexes with Co(II)‐isoenzymes I and II. The spectrum of the N − 3 complex indicates that this anion is bound somewhat differently in Co(II) isoenzyme III than in the other Co(II)‐substituted isoenzymes.