These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Binding of Al(III)-tetracarboxyphthalocyanine to hemoglobin and myoglobin.
    Author: Zhou QH, Zhang HM, Wu L, Wang YQ.
    Journal: Protein J; 2010 May; 29(4):265-75. PubMed ID: 20496102.
    Abstract:
    The interactions between Al(III)-tetracarboxyphthalocyanine (AlPc(COOH)(4)) and hemoglobin (or myoglobin) have been studied. The results showed that AlPc(COOH)(4) effectively quenched the intrinsic fluorescence of Hb and Mb via static quenching. The hydrophobic and electrostatic interactions played a major role in stabilizing the AlPc(COOH)(4)-protein complex. The distance r between donor and acceptor was obtained to be 3.92 and 3.67 nm for AlPc(COOH)(4)-Hb and AlPc(COOH)(4)-Mb system, respectively. The effect of AlPc(COOH)(4) on the conformation of Hb and Mb was analyzed using UV-vis absorption spectroscopy, circular dichroism spectra, synchronous fluorescence and three-dimensional fluorescence spectra.
    [Abstract] [Full Text] [Related] [New Search]