Please use this identifier to cite or link to this item:
|Title: ||Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe|
|Authors: ||Silva, Gabriela|
Xavier, António V.
|Keywords: ||Desulfovibrio gigas|
|Issue Date: ||1999|
|Abstract: ||Neelaredoxin, a small non-heme blue iron protein from the sulfate-reducing bacterium Desulfovibrio gigas [Chen,
L., Sharma, P., LeGall, J., Mariano, A.M., Teixeira M. and Xavier, A.V. (1994) Eur. J. Biochem. 226, 613±618] is
shown to be encoded by a polycistronic unit which contains two additional open reading frames (ORF-1 and ORF-2)
coding for chemotaxis-like proteins. ORF-1 has domains highly homologous with those structurally and functionally
important in methyl-accepting chemotaxis proteins, including two putative transmembrane helices, potential
methylation sites and the interaction domain with CheW proteins. Interestingly, ORF-2 encodes a protein having
homologies with CheW proteins.
Neelaredoxin is also shown to have significant superoxide dismutase activity (1200 U´mg±1), making it a novel
type of iron superoxide dismutase. Analysis of genomic data shows that neelaredoxin-like putative polypeptides are
present in strict anaerobic archaea, suggesting that this is a primordial superoxide dismutase.
The three proteins encoded in this operon may be involved in the oxygen-sensing mechanisms of this anaerobic
bacterium, indicating a possible transcriptional mechanism to sense and respond to potential stress agents.|
|Appears in Collections:||MED - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica|
BIO - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.