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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

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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… Expand
Highly Cited
2006
Highly Cited
2006
Roles of the Host Oxidative Immune Response and Bacterial Antioxidant Rubrerythrin during Porphyromonas gingivalis Infection
The efficient clearance of microbes by neutrophils requires the concerted action of reactive oxygen species and microbicidal… Expand
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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… Expand
Highly Cited
2001
Highly Cited
2001
Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system.
Evidence is presented for an alternative to the superoxide dismutase (SOD)-catalase oxidative stress defense system in… Expand
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Highly Cited
2001
Highly Cited
2001
A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase.
Desulfovibrio vulgaris rubredoxin, which contains a single [Fe(SCys)4] site, is shown to be a catalytically competent electron… Expand
Highly Cited
1997
Highly Cited
1997
Mössbauer studies of alkane omega-hydroxylase: evidence for a diiron cluster in an integral-membrane enzyme.
The gene encoding the alkane omega-hydroxylase (AlkB; EC 1.14.15.3) from Pseudomonas oleovorans was expressed in Escherichia coli… Expand
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Highly Cited
1996
Highly Cited
1996
Rubrerythrin from Clostridium perfringens: cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function.
The food-borne pathogen Clostridium perfringens, which is an obligate anaerobe, showed growth under conditions of oxidative… Expand
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… Expand
1996
1996
Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin
Abstract Rubrerythrin (Rr) is the trivial name given to a non-heme iron protein of unknown function which has been found in… Expand
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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… Expand
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