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The Sporomusa type Nfn is a novel type of electron-bifurcating transhydrogenase that links the redox pools in acetogenic bacteria.
- Source :
-
Scientific reports [Sci Rep] 2020 Sep 10; Vol. 10 (1), pp. 14872. Date of Electronic Publication: 2020 Sep 10. - Publication Year :
- 2020
-
Abstract
- Flavin-based electron bifurcation is a long hidden mechanism of energetic coupling present mainly in anaerobic bacteria and archaea that suffer from energy limitations in their environment. Electron bifurcation saves precious cellular ATP and enables lithotrophic life of acetate-forming (acetogenic) bacteria that grow on H <subscript>2</subscript> + CO <subscript>2</subscript> by the only pathway that combines CO <subscript>2</subscript> fixation with ATP synthesis, the Wood-Ljungdahl pathway. The energy barrier for the endergonic reduction of NADP <superscript>+</superscript> , an electron carrier in the Wood-Ljungdahl pathway, with NADH as reductant is overcome by an electron-bifurcating, ferredoxin-dependent transhydrogenase (Nfn) but many acetogens lack nfn genes. We have purified a ferredoxin-dependent NADH:NADP <superscript>+</superscript> oxidoreductase from Sporomusa ovata, characterized the enzyme biochemically and identified the encoding genes. These studies led to the identification of a novel, Sporomusa type Nfn (Stn), built from existing modules of enzymes such as the soluble [Fe-Fe] hydrogenase, that is widespread in acetogens and other anaerobic bacteria.
- Subjects :
- Acetobacterium genetics
Adenosine Triphosphate metabolism
Amino Acid Sequence
Anaerobiosis
Bacterial Proteins genetics
Bacterial Proteins isolation & purification
Electron Transport
Electrons
Firmicutes genetics
Hydrogenase genetics
Hydrogenase isolation & purification
Iron-Sulfur Proteins genetics
Iron-Sulfur Proteins isolation & purification
Oxidation-Reduction
Sequence Homology, Amino Acid
Acetobacterium enzymology
Bacterial Proteins metabolism
Ferredoxins metabolism
Firmicutes enzymology
Hydrogenase metabolism
Iron-Sulfur Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 10
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 32913242
- Full Text :
- https://doi.org/10.1038/s41598-020-71038-2