Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum

Two flavo-diiron proteins (FDPs), FprA1 and FprA2, are up-regulated when the strictly anaerobic solvent producer, Clostridium acetobutylicum, is exposed to dioxygen. These two FDPs were purified following heterologous overexpression in Escherichia coli as N-terminal Strep-tag fusion proteins. The re...

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Bibliographic Details
Published in:FEBS letters 2009-01, Vol.583 (1), p.241-245
Main Authors: Hillmann, Falk, Riebe, Oliver, Fischer, Ralf-Jörg, Mot, Augustin, Caranto, Jonathan D., Kurtz, Donald M., Bahl, Hubert
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Clostridium acetobutylicum
Clostridium acetobutylicum - enzymology
Clostridium acetobutylicum - genetics
Dimerization
Escherichia coli
Escherichia coli - genetics
Flavo-diiron
Flavoproteins - chemistry
Flavoproteins - genetics
Flavoproteins - metabolism
Molecular Sequence Data
NADH, NADPH Oxidoreductases - chemistry
NADH, NADPH Oxidoreductases - genetics
NADH, NADPH Oxidoreductases - metabolism
Nitric Oxide - chemistry
Nitric Oxide - metabolism
O2 reduction
Oxidation-Reduction
Oxygen - chemistry
Oxygen - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Rubredoxin
Rubredoxins - genetics
Rubredoxins - metabolism
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Summary:Two flavo-diiron proteins (FDPs), FprA1 and FprA2, are up-regulated when the strictly anaerobic solvent producer, Clostridium acetobutylicum, is exposed to dioxygen. These two FDPs were purified following heterologous overexpression in Escherichia coli as N-terminal Strep-tag fusion proteins. The recombinant FprA1 and FprA2 were found to be homodimeric and homotetrameric, respectively, and both FDPs functioned as terminal components of NADH oxidases (NADH:O2 oxidoreductases) when using C. acetobutylicum NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries. Both FDPs catalyzed the four-electron reduction of molecular oxygen to water with similar specific activities. The results are consistent with these FDPs functioning as efficient scavengers of intracellular dioxygen under aerobic or microoxic growth conditions.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2008.12.004