Metal-binding properties of human erythrocyte carbonic anhydrases

Lindskog, Sven; Nyman, Per Olof

doi:10.1016/0926-6569(64)90310-4

Cited by 134 publications

(152 citation statements)

References 23 publications

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“…The spectra of the adducts of Co(H)-isoenzyme III with acetazolamide, CN-and NCO-are virtually identical to the corresponding spectra obtained with Co(II)-isoenzymes I and II [17,19,20,251, again implying similar structures of the metal ion centers in the three isoenzymes. This is particularly interesting in the case of acetazolamide since this sulfonamide inhibitor binds much more weakly to isoenzyme III than to isoenzymes I and II.…”

Section: Discussionsupporting

confidence: 55%

Effects of pH and inhibitors on the absorption spectrum of cobalt(II)‐substituted carbonic anhydrase III from bovine skeletal muscle

Engberg¹,

Lindskog²

1984

FEBS Letters

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Bovine apocarbonic anhydrase III has been prepared by incubation with 2-c~boxy-l,lO-phenanthroIine 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 NS complex indicates that this anion is bound somewhat differently in Co(H) isoenzyme III than in the other Co(II)-substituted isoenzymes. Carbonic anhydrase Isoenzyme Muscle

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Section: Discussionsupporting

confidence: 55%

Effects of pH and inhibitors on the absorption spectrum of cobalt(II)‐substituted carbonic anhydrase III from bovine skeletal muscle

Engberg¹,

Lindskog²

1984

FEBS Letters

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“…8 It is likely that in sea-water the complexation is subject to competition by the major cations which would tend to lower the apparent complex stability. The lower complex stability found in this work is therefore in line with expectation.…”

Section: Discussionmentioning

confidence: 99%

“…It has been shown that the interaction of metals with human apocarbonic anhydrase B is reversible, resembling metal complexes: 8 zinc could be taken out of the enzyme, causing the activity to decrease, and the activity could be restored by adding cobalt which replaced the zinc. The complex stability of human CA is known to be strong, even leading to the suggestion that it could be used as a Zn 2+ sensor.…”

Section: Introductionmentioning

confidence: 99%

Determination of the complex stability of zinc with carbonic anhydrase in sea-water

Sarthou

Berg

Riebesell

2001

Analyst

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Carbonic anhydrase (CA) is inactive unless associated with zinc, with possible substitution by cobalt. In this work, the complexation of zinc by CA was determined in sea-water using cathodic stripping voltammetry (CSV) with ligand competition. The zinc was found to be released from the CA over a period of 3 h when equilibrated with a competing complexing ligand and the complex was re-formed with the CA when zinc was added. A value of 8.90 ± 0.27 was found for logKA ZnCA where KA ZnCA is the conditional stability constant for the complex of Zn 2+ with CA in pH 8 sea-water. A value for the molecular weight of CA was calculated from its equivalent ligand concentration (in nM) obtained by titrations with zinc at various CA concentrations (1-4 mg l 21 ). The value found (34740 g mol 21 ) for the molecular weight is consistent with values found previously by other methods (29000-31000 g mol 21 ) confirming that the stoichiometry of the complex between zinc and CA is 1+1. This work confirms that the zinc-CA complex is reversible and that the interaction between zinc and CA can be determined using CSV with ligand competition.

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“…Similar comparisons of the bonding geometry of copper(II) and zinc in complexes with biological ligands had either yielded closely similar structures in the case of glutamic acid (Gramaccioli, 1966;Gramaccioli & Marsh, 1966) or, with L-serine, structures with small but distinct differences (Van der Helm & Franks, 1969; Van der Helm, Nicholas & Fisher, 1970). In addition metal replacement studies show that copper(II) often inactivates zinc enzymes (Vallee, Riordan & Colman, 1964;Linskog & Nyman, 1964;Plocke & VaUee, 1962).…”

Section: Introductionmentioning

confidence: 99%

The crystal and molecular structure of diaquo(glycylglycylglycinato)zinc hemisulfate dihydrate

Helm¹,

Nicholas²

1970

Acta Crystallogr Sect B

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The crystal structure of diaquo zinc glycylglycylglycinato hemisulfate dihydrate, Zn(N3C604Hlo) (H20)4 (SO4)i/2, has been determined and refined by three-dimensional least-squares techniques, using 2095 counter data.The crystals are orthorhombic, space group Pbcn, with a= 25.86, b = 8.011 and c = 13.59 A. The final R value for 2095 reflections is 0"065. The standard deviations are about 0.005/~ for the light atom positions. The zinc surrounding is better described as a trigonal bipyramid than as a square pyramid. The peptide molecules form infinite chains held together by zinc ions.

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Metal-binding properties of human erythrocyte carbonic anhydrases

Cited by 134 publications

References 23 publications

Effects of pH and inhibitors on the absorption spectrum of cobalt(II)‐substituted carbonic anhydrase III from bovine skeletal muscle

Effects of pH and inhibitors on the absorption spectrum of cobalt(II)‐substituted carbonic anhydrase III from bovine skeletal muscle

Determination of the complex stability of zinc with carbonic anhydrase in sea-water

The crystal and molecular structure of diaquo(glycylglycylglycinato)zinc hemisulfate dihydrate

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