A Novel Type of Nitric-oxide Reductase

@article{Gomes2002ANT,
  title={A Novel Type of Nitric-oxide Reductase},
  author={Cl{\'a}udio M. Gomes and Alessandro Giuffr{\`e} and Elena Forte and Jo{\~a}o B Vicente and L{\'i}gia M. Saraiva and Maurizio Brunori and Miguel Teixeira},
  journal={The Journal of Biological Chemistry},
  year={2002},
  volume={277},
  pages={25273 - 25276}
}
Escherichia coli flavorubredoxin is a member of the family of the A-type flavoproteins, which are built by two core domains: a metallo-β-lactamase-like domain, at the N-terminal region, harboring a non-heme di-iron site, and a flavodoxin-like domain, containing one FMN moiety. The enzyme fromE. coli has an extra module at the C terminus, containing a rubredoxin-like center. The A-type flavoproteins are widespread among strict and facultative anaerobes, as deduced from the analysis of the… Expand
Structure of Escherichia coli Flavodiiron Nitric Oxide Reductase.
TLDR
The present data represent the first structure for a NO-selective FDP, and only the flavodiiron domain was observed in these crystal structures, while the structure of the rubredoxin domain was determined by NMR. Expand
The role of the flavodiiron proteins in microbial nitric oxide detoxification.
TLDR
This review will discuss available data for this novel family of enzymes, including their physicochemical properties, structural and phylogenetic analyses, enzymatic properties and the molecular genetic approaches so far used to tackle their function. Expand
Flavodiiron Proteins: Nitric Oxide and/or Oxygen Reductases
Flavodiiron proteins (FDPs) have been isolated from and identified in genomes of bacteria, archaea, and a restricted group of pathogenic protozoa, mostly anaerobes or microaerophiles. The currentExpand
Diversity and complexity of flavodiiron NO/O2 reductases.
TLDR
Following an extensive analysis of genomic databases, novel domain compositions are identified, and a new classification of FDPs in eight classes based on the nature and number of extra domains is proposed. Expand
Gene expression study of the flavodi-iron proteins from the cyanobacterium Synechocystis sp. PCC6803.
TLDR
One of the flavodi-iron genes, the so-called flv1, is induced in cells exposed to nitrosative stress and is identified that the FDPs of cyanobacteria and oxygenic photosynthetic eukaryotes may be divided into multiple types according to the amino acid residues of the di-iron catalytic site. Expand
“STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF ESCHERICHIA COLI FLAVOHEMOGLOBIN”. ALESSANDRA BONAMORE
  • 2005
Flavohemoglobins are oxygen binding proteins composed of a heme-containing globin domain fused with a ferredoxin reductase-like FADand NAD-binding domain. Genes codifing for these proteins have beenExpand
Redox and Spectroscopic Properties of the Escherichia coli Nitric Oxide-detoxifying System Involving Flavorubredoxin and Its NADH-oxidizing Redox Partner*
TLDR
The first direct EPR evidence for the presence of the non-heme diiron site in the flavodiiron proteins family is presented, and it is shown that the redox properties of this complex electron transfer system are fine-tuned upon interaction of the two enzymes. Expand
Desulforubrerythrin from Campylobacter jejuni, a novel multidomain protein
TLDR
A novel multidomain metalloprotein from Campylobacter jejuni was overexpressed in Escherichia coli, purified, and extensively characterized, and represents a novel example of the large diversity of the organization of domains exhibited by this enzyme family. Expand
Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type.
  • W. Zumft
  • Chemistry, Medicine
  • Journal of inorganic biochemistry
  • 2005
TLDR
There is currently a broadening of the scope of NO functionality and an increase in awareness that other heme-based NO-metabolizing systems contribute to the overall capability of the prokaryotic cell to cope with NO both in anaerobic and aerobic environments, including the pathogen-host interface. Expand
Biochemical, spectroscopic, and thermodynamic properties of flavodiiron proteins.
TLDR
Spectroscopic techniques, namely absorption and near-ultraviolet and electron paramagnetic resonance spectroscopies, allowed redox-sensitive spectral fingerprints to be obtained and used further in the functional characterization of isolated flavodiiron proteins. Expand
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