Literature DB >> 3816780

Fluctuation domains in myoglobin. Fluorescence quenching studies.

J Albani, B Alpert.   

Abstract

The dynamics of two domains in the myoglobin molecule, close to the heme and inside the protein medium including the surface, are investigated through the study of the fluorescence oxygen quenching of two probes imbedded in the heme pocket: zinc protoporphyrin IX (with a fluorescence lifetime of 2.1 ns) and metal-free protoporphyrin IX (with a fluorescence lifetime of 17.8 ns).

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Year:  1987        PMID: 3816780     DOI: 10.1111/j.1432-1033.1987.tb10558.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  2 in total

1.  Reactions of excited triplet states of metal substituted myoglobin with dioxygen and quinone.

Authors:  S Papp; J M Vanderkooi; C S Owen; G R Holtom; C M Phillips
Journal:  Biophys J       Date:  1990-07       Impact factor: 4.033

2.  Photoactivation studies of zinc porphyrin-myoglobin system and its application for light-chemical energy conversion.

Authors:  Chin-Hao Chang; Yi-Ting Hu; Chen-Fu Lo; Liyang Luo; Hung-Ming Lin; Cheng-Hsiang Chang; Ching-Yao Lin; Eric Wei-Guang Diau; Tung-Kung Wu
Journal:  Int J Biol Sci       Date:  2011-10-27       Impact factor: 6.580

  2 in total

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