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A third subunit in ancestral cytochrome c-dependent nitric oxide reductases.
- Source :
-
Applied and environmental microbiology [Appl Environ Microbiol] 2014 Aug; Vol. 80 (16), pp. 4871-8. Date of Electronic Publication: 2014 Jun 06. - Publication Year :
- 2014
-
Abstract
- Reduction of NO to N2O by denitrifiying bacteria is catalyzed either by a monomeric quinol-nitric oxide reductase (qNor) or by a heterodimeric cytochrome c-dependent nitric oxide reductase (cNor). In ancient thermophilic bacteria belonging to the Thermales and Aquificales phylogenetic groups, the cluster encoding the cNor includes a small third gene (norH), in addition to those encoding homologues to the subunits of a typical cNor (norC and norB). We show in Thermus thermophilus that the three genes are cotranscribed in a single mRNA from an inducible promoter. The isolation of individual nor mutants and the production in vivo of His-tagged NorH protein followed by immobilized-metal affinity chromatography (IMAC) allowed us to conclude that NorH constitutes a third subunit of the cNor from T. thermophilus, which is involved in denitrification in vivo, likely allowing more efficient electron transport to cNor.<br /> (Copyright © 2014, American Society for Microbiology. All Rights Reserved.)
- Subjects :
- Bacterial Proteins chemistry
Bacterial Proteins genetics
Nitric Oxide metabolism
Operon
Oxidoreductases chemistry
Oxidoreductases genetics
Promoter Regions, Genetic
Protein Subunits chemistry
Protein Subunits genetics
Sequence Homology, Amino Acid
Thermus thermophilus chemistry
Thermus thermophilus genetics
Thermus thermophilus metabolism
Bacterial Proteins metabolism
Cytochromes c metabolism
Oxidoreductases metabolism
Protein Subunits metabolism
Thermus thermophilus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5336
- Volume :
- 80
- Issue :
- 16
- Database :
- MEDLINE
- Journal :
- Applied and environmental microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 24907324
- Full Text :
- https://doi.org/10.1128/AEM.00790-14