The 1.6 Å resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-06-24

AUTHORS

Cheryl A. Kerfeld, Stephanie Yoshida, Kimberlee T. Tran, Todd O. Yeates, Duilio Cascio, Hervé Bottin, Catherine Berthomieu, Miwa Sugiura, Alain Boussac

ABSTRACT

The iron-containing superoxide dismutase (FeSOD) from the thermophilic cyanobacterium Thermosynechococcus elongatus has been isolated. The protein crystallizes readily and we have determined the structure to 1.6 Å resolution. This is the first structural characterization of an FeSOD isolated from a cyanobacterium and one of the highest resolution FeSOD structures determined to date. The activity of the T. elongatus FeSOD has been measured both at 25 °C and 50 °C and it has been spectroscopically characterized. The T. elongatus FeSOD EPR spectra at pH 5.1, 7.5 and 10.0 are similar. This indicates that no change in the geometry of the FeIII site occurs over a wide range of pH. This is in contrast to the other FeSODs described in the literature. More... »

PAGES

707-714

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00775-003-0469-0

DOI

http://dx.doi.org/10.1007/s00775-003-0469-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038985148

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12827458


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