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rubrerythrins

Known as: rubrerythrin, rubrerythrin proteins 
National Institutes of Health

Related topics

Related topics

2 relations

Broader (2)

HemerythrinRubredoxins

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2010
Review
2010
The Ferritin-like superfamily: Evolution of the biological iron storeman from a rubrerythrin-like ancestor.
  • S. Andrews
  • Biochimica et Biophysica Acta
  • 2010
  • Corpus ID: 6897748
Highly Cited
2009
Highly Cited
2009
Something Old, Something New, Something Borrowed; How the Thermoacidophilic Archaeon Sulfolobus solfataricus Responds to Oxidative Stress
To avoid molecular damage of biomolecules due to oxidation, all cells have evolved constitutive and responsive systems to… 
Highly Cited
2004
Highly Cited
2004
Rubrerythrin from the Hyperthermophilic Archaeon Pyrococcus furiosus Is a Rubredoxin-Dependent, Iron-Containing Peroxidase
ABSTRACT Rubrerythrin was purified by multistep chromatography under anaerobic, reducing conditions from the hyperthermophilic… 
Highly Cited
2002
Highly Cited
2002
Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis
Rubrerythrins are non‐haem iron proteins that have been implicated in oxidative stress protection in anaerobic bacteria and… 
Highly Cited
2002
Highly Cited
2002
Computational de novo design, and characterization of an A(2)B(2) diiron protein.
Highly Cited
2002
Highly Cited
2002
X-ray crystal structures of reduced rubrerythrin and its azide adduct: a structure-based mechanism for a non-heme diiron peroxidase.
Rubrerythrin (Rbr) is a 44-kDa homodimeric protein, found in many air-sensitive bacteria and archaea, which contains a unique… 
Highly Cited
2001
Highly Cited
2001
Rubrerythrin and Rubredoxin Oxidoreductase inDesulfovibrio vulgaris: a Novel Oxidative Stress Protection System
ABSTRACT Evidence is presented for an alternative to the superoxide dismutase (SOD)-catalase oxidative stress defense system… 
Review
2000
Review
2000
New insight into the structure and function of the alternative oxidase.
Highly Cited
1996
Highly Cited
1996
The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains
We have determined the structure of rubrerythrin, a non-haem iron protein from the anaerobic sulphate-reducing bacterium… 
Highly Cited
1988
Highly Cited
1988
Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster.
A new non-heme iron protein from the periplasmic fraction of Desulfovibrio vulgaris (Hildenbourough NCIB 8303) has been purified… 
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