The replacement of calcium by terbium as an allosteric effector of hemocyanins

Kuiper, H.A.; Agró, Alessandro Finazzi; Antonini, Eraldo; Brunori, Maurizio

doi:10.1016/0014-5793(79)80981-3

Cited by 17 publications

(2 citation statements)

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“…As a final remark it should be pointed out that no quenching of CO-linked phosphorescence was observed upon addition of Tb(III) or Eu(III), which suggests that cation binding sites are removed from the copper centers. Moreover the latter sites have been found largely accessible to water (Kuiper et al, 1979) while the copper centers seem to be shielded from the solvent, as already proposed (Alben et al, 1970).…”

Section: Discussionsupporting

confidence: 61%

“…Effect of Ca(IT) and Lanthanides on CO Emission. We have described the binding of several lanthanides to deoxyhemocyanin and obtained evidence that some of them occupy the Ca(II) binding sites (Kuiper et al, 1979(Kuiper et al, ,1981. Tb(III) shows a protein-sensitized emission while other lanthanides only induce a quenching of protein and/or bound Tb(III) emission.…”

Section: Resultsmentioning

confidence: 99%

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Spectroscopy of carbon monoxide-hemocyanins. Phosphorescence of the binuclear carbonylated copper centers

Finazzi‐Agrò¹,

Zolla²,

Flamigni³

et al. 1982

Biochemistry

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The luminescence of CO-hemocyanin has been studied in several hemocyanins from both arthropods and molluscs. All of them show an emission in the region 550-560 nm with quantum yield = 0.2-0.4, though individual differences are apparent. Solvent composition (as well as the presence of calcium and lanthanides) has no effect on the emission. Lifetimes of this luminescence are in the range 60-140 microseconds, indicating that the emitting state may be a triplet. The presence of both copper atoms (Cu+) per CO binding site is required for the luminescent state since half-met and half-apo derivatives do not show such an emission. Though not clearly related to any of the functional properties, systematic differences in luminescence parameters are apparent between arthropodal and molluscan hemocyanins. Limulus hemocyanin appears to be very different from both types of hemocyanin.

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Section: Discussionsupporting

confidence: 61%

Section: Resultsmentioning

confidence: 99%