The iron-sulfur flavoprotein complex, originally isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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SYSTEMATIC NAME
IUBMB Comments
NADH:NADP+, ferredoxin oxidoreductase
The iron-sulfur flavoprotein complex, originally isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH.
reduction of both NAD+ and Fd by Nfn enzymes is coupled to the bifurcation of electrons from NADPH oxidation. The exergonic coupling of the NADP(H) and NAD(H) half reactions in Nfn is presumed to be mediated by NADPH oxidation at L-FAD followed by electron transfer to the proximal [2Fe-2S] cluster and subsequently the NAD(H) binding site at S-FAD. Biophysical analysis of the enzyme provides the first direct insight into the mechanism of flavin-based electron bifurcation and the requisite structural features
in the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+). In the absence of ferredoxin, NAD+ is only very slowly reduced (less than 1% of the rate observed in the presence of ferredoxin)
in the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+). In the absence of ferredoxin, NAD+ is only very slowly reduced (less than 1% of the rate observed in the presence of ferredoxin)
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH. In the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+)
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH. In the absence of NAD+, ferredoxin is only very slowly reduced (0.5% of the rate seen in the presence of NAD+)
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
the iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH
the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster. The [2Fe-2S] cluster is unusual, with a relatively high (positive) reduction potential and coordination by one Asp and three Cys ligands
the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster with an unusual Asp ligand. The 53000 Da subunit contains one FAD (L-FAD), which is the site of electron bifurcation, and two [4Fe-4S] clusters. The L-FAD proximal [4Fe-4S] cluster coordination includes an unusual Glu ligand. S-FAD and L-FAD bind NADH and NADPH, respectively
iron-sulfur flavoprotein complex, subunit NfnA has a predicted [2Fe2S] binding site, subunit NfnB has two predicted [4Fe4S] binding sites. UV-visible spectrum shows that the NfnAB complex contains up to 10 Fe molecules per heterodimer, which is consistent with the presence of two [4Fe4S] and one [2Fe2S] clusters
the enzyme has a key role in maintaining redox homeostasis. It is involved in maintaining the cellular redox balance, producing NADPH for biosynthesis by recycling the two other primary redox carriers, NADH and ferredoxin. The enzyme effectively couples the endergonic reduction of NADP+ by NADH and the exergonic reduction of NADP+ by reduced ferredoxin, thereby maintaining a high ratio of NADPH/NADP+ to drive biosynthesis. The Pyrococcus furiosus genome encodes an NfnI paralog termed NfnII, and the two are differentially expressed, depending on the growth conditions. Deletion of the genes encoding either NfnI or NfnII affects the cellular concentrations of NAD(P)H and particularly NADPH. This results in a moderate to severe growth phenotype in deletion mutants, demonstrating a key role for each enzyme in maintaining redox homeostasis
improvement of hydrogen production is achieved by overexpression of membrane-integral nicotinamide nucleotide transhydrogenase PntAB and deletion of soluble pyridine nucleotide transhydrogenase SthA. A 3.9fold increased hydrogen yield is observed
Purification of a flavoprotein having NADPH-cytochrome c reductase and transhydrogenase activities from Nitrobacter winogradskyi and its molecular and enzymatic properties