Two copper proteins azurin-1 and azurin-2 were isolated from denitrifying bacteria Alcaligenes xylosoxidans GIFU1051, and the mass spectrometric analysis of the proteins were carried out by both matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) and electrospray ionization (ESI).
An ENDOR and ESEEM study of the blue copper protein azurin
β Scribed by J.W.A. Coremans; M. van Gastel; O.G. Poluektov; E.J.J. Groenen; T. den Blaauwen; G. van Pouderoyen; G.W. Canters; H. Nar; C. Hammann; A. Messerschmidt
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 682 KB
- Volume
- 235
- Category
- Article
- ISSN
- 0009-2614
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β¦ Synopsis
We report electron-nuclear double-resonance experiments on a single crystal of azurin at 95 GHz and electron-spin-echo envelope-modulation experiments on frozen solutions of azurin and of the H117G mutant at 9 GHz. The hyperfine and quadrupole tensors of the two remote nitrogens of the histidine ligands of copper are assigned and discussed. A third nucleus is found to contribute to the echo-modulation spectrum and this probably concerns an amide nitrogen of the peptide backbone.
π SIMILAR VOLUMES
1 H-and 13 C-NMR spectroscopy is applied to investigate the Cu A and type 1 active sites of copper proteins in solution. The analysis of hyperfine shifted 1 H resonances allows the comparison of the electron spin density delocalization in the Cu A site of the wild-type soluble domains of various cyt
## Abstract ^1^Hβ and ^14^Nβcoupling constants have been determined by ESR. and ENDOR. spectroscopy for the radical anions of 1β and 2βcyanoβ, and 1β and 2βnitronaphthalene.