Open AccessLuminescence of carbon monoxide hemocyanins.
Author(s) -
H.A. Kuiper,
Alessandro Finazzi Agrò,
Eraldo Antonini,
Maurizio Brunori
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.5.2387
Subject(s) - carbon monoxide , luminescence , hemocyanin , photochemistry , titration , chemistry , fluorescence , emission spectrum , helix pomatia , analytical chemistry (journal) , spectral line , materials science , inorganic chemistry , biology , biochemistry , organic chemistry , optics , optoelectronics , physics , ecology , astronomy , antigen , snail , genetics , catalysis
The effect of carbon monoxide on the luminescence properties of Helix pomatia alpha-hemocyanin and Panulirus interruptus hemocyanin has been studied. These proteins, when saturated with carbon monoxide, show, besides the intrinsic fluorescence arising from the aromatic amino acid residues, emission in the visible region with a maximum between 540 and 560 nm. Results of carbon monoxide titration experiments and data from absorption and excitation-emission spectra provide convincing evidence that the observed emission originates from a fluorescent copper(I)-carbon monoxide complex, and this emission is interpreted as charge-transfer luminescence.