Complexation of Copper(II) Ion with Tetraglycine as Followed by Electronic Absorption Spectroscopy. A Bioinorganic Chemistry Experiment

Eugenio Garribba and Giovanni Micera
Department of Chemistry, University of Sassari, I-07100 Sassari, Italy
J. Chem. Educ., 2007, 84 (5), p 832
DOI: 10.1021/ed084p832
Publication Date (Web): May 1, 2007

Abstract

The complexation of Cu(II) ion with tetraglycine (TetraGly) is studied by electronic absorption spectroscopy as a function of pH. In an equimolar solution, tetraglycine forms a sequence of 1:1 chelated species: [CuL]+ around pH 5.4, [CuLH-1] around pH 6.4, [CuLH-2]- around pH 8.0, and [CuLH-3]2- above pH 11.0. They are characterized, respectively, by the equatorial donor sets [(NH2, CO); H2O; H2O], [(NH2, N-, CO); H2O], [NH2, N-, N-, CO], and [NH2, N-, N-, N-], where NH2 is the amino, CO the carbonyl, and N- the deprotonated amide group. The electronic absorption spectra exhibit a single band in the visible region, which becomes sharper and shifts to higher energy values as the complexation proceeds and the water molecules are replaced by stronger donors. The experimental λmax value can be calculated through Billo's equation, which assigns a different contribution to the equatorial water, carbonyl-O, carboxylate-O, amino-N, and deprotonated amide-N. Two biological applications, the interaction of Cu(II) with prion and the transport of copper by albumin, are presented.

Keywords (Audience):

Upper-Division Undergraduate

Keywords (Domain):

Biochemistry

Keywords (Pedagogy):

Hands-On Learning / Manipulatives

Keywords (Subject):

Aqueous Solution Chemistry

Citing Articles

Citation data is made available by participants in CrossRef's Cited-by Linking service. For a more comprehensive list of citations to this article, users are encouraged to perform a search in SciFinder.

This article has been cited by 1 ACS Journal articles (1 most recent appear below).

  • Cover Image

    Using Proteins in a Bioinorganic Laboratory Experiment: Iron Loading and Removal from Transferrin

    David H. Hamilton , Erin E. Battin , Ashley Lawhon and Julia L. Brumaghim
    Journal of Chemical Education2009 86 (8), 969
    • Using Proteins in a Bioinorganic Laboratory Experiment: Iron Loading and Removal from Transferrin

      David H. Hamilton , Erin E. Battin , Ashley Lawhon and Julia L. Brumaghim
      Journal of Chemical Education2009 86 (8), 969

      With the increasing availability of metalloproteins it is now possible to incorporate them into bioinorganic laboratory experiments. Thus, we have developed a laboratory experiment where students use UV–vis spectroscopy to determine the rate of iron ...

Tools

SciFinder Links

SciFinder subscribers:  Click to sign in | Not a SciFinder subscriber? Learn more at www.cas.org

Explore by:


History

  • Received: August 03, 2009

Recommend & Share

  • Share on ACS NetworkACS Network
  • Add to FacebookFacebook
  • Tweet ThisTweet This
  • Add to CiteULikeCiteULike
  • Add to NewsvineNewsvine
  • Digg ThisDigg This
  • Add to DeliciousDelicious

Related Content