Journal
FEBS LETTERS
Volume 583, Issue 1, Pages 241-245Publisher
WILEY
DOI: 10.1016/j.febslet.2008.12.004
Keywords
Clostridium acetobutylicum; O-2 reduction; Flavo-diiron; Rubredoxin
Funding
- SysMO project COSMIC
- NIH [GM040388]
- Graduiertenforderung of the Federal State of Mecklenburg-Vorpommern
- Romanian Ministry for Education and Research [PN-II-Ideas-107/2007]
Ask authors/readers for more resources
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: O-2 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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available