Literature DB >> 2545268

Analytical characterization of cytochrome oxidase preparations with regard to metal and phospholipid contents, peptide composition and catalytic activity.

M Oblad1, E Selin, B Malmström, L Strid, R Aasa, B G Malmström.   

Abstract

A number of preparations of cytochrome oxidase have been analyzed for metals by energy dispersive X-ray fluorescence spectrometry. The EPR characteristics, the peptide compositions, the protein and phospholipid contents as well as the catalytic constants of the samples have also been determined. It is confirmed that the enzyme functional unit contains three copper atoms and one zinc atom in addition to two iron atoms. On the basis of the parameters determined for the different samples it is suggested that a high catalytic activity of a preparation can be correlated to a number of other analytical characteristics.

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Year:  1989        PMID: 2545268     DOI: 10.1016/s0005-2728(89)80257-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

Review 1.  Cytochrome c oxidase metal centers: location and function.

Authors:  M Müller; A Azzi
Journal:  J Bioenerg Biomembr       Date:  1991-04       Impact factor: 2.945

Review 2.  Current issues in the chemistry of cytochrome c oxidase.

Authors:  G Palmer
Journal:  J Bioenerg Biomembr       Date:  1993-04       Impact factor: 2.945

Review 3.  Cu(A) centers and their biosynthetic models in azurin.

Authors:  Masha G Savelieff; Yi Lu
Journal:  J Biol Inorg Chem       Date:  2010-02-19       Impact factor: 3.358

4.  Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex.

Authors:  J van der Oost; P Lappalainen; A Musacchio; A Warne; L Lemieux; J Rumbley; R B Gennis; R Aasa; T Pascher; B G Malmström
Journal:  EMBO J       Date:  1992-09       Impact factor: 11.598

  4 in total

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