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- Publisher
- Wiley
- Copyright
- Copyright © 2004 Wiley Periodicals, Inc., A Wiley Company
- ISSN
- 0006-3525
- eISSN
- 1097-0282
- DOI
- 10.1002/bip.20045
- pmid
- 15137096
- Publisher site
- See Article on Publisher Site
Abstract
CD spectroscopic study of the secondary structure of partly adenylylated glutamine synthetase (GS) of the bacterium Azospirillum brasilense showed both the native and cation‐free (EDTA‐treated) enzyme to be highly structured (58 and 49% as α‐helices, 10 and 20% as β‐structure, respectively). Mg2+, Mn2+, or Co2+, when added to the native GS, had little effect on its CD spectrum, whereas their effects on the cation‐free GS were more pronounced. Emission (57Co) Mössbauer spectroscopic (EMS) study of 57Co2+‐doped cation‐free GS in frozen solution and in the dried state gave similar spectra and Mössbauer parameters for the corresponding spectral components, reflecting the ability of the Co2+–enzyme complex to retain its properties upon drying. The EMS data show that (a) A. brasilense GS has 2 cation‐binding sites per active center and (b) one site has a higher affinity to Co2+ than the other, in line with the data on other bacterial GSs. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004
Journal
Biopolymers – Wiley
Published: May 1, 2004
Keywords: glutamine synthetase; Azospirillum brasilense; secondary structure; active center; CD; 57 Co emission Mössbauer spectroscopy