Ferredoxin NADP+ Reductase: Difference between revisions

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Rebecca Truitt, Dana Emmert, Michal Harel, Jaime Prilusky, Alexander Berchansky

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-ferredoxin NADP+ reductase [http://en.wikipedia.org/wiki/Ferredoxin—NADP(%2B)_reductase] is an enzyme that catalyzes the reduction of NADP+ to NADPH.  This enzyme belongs to a family of enzymes called oxidoreductases (link to Wiki) that contain iron-sulfur proteins as electron donors and NAD+ or NADP+ as electron acceptors. FAD, [flavin adenine dinucleotide][http://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide], is also a cofactor of FNR. The ferredoxin NADP+ reductase participates in a general reaction that proceeds as follows:
+ferredoxin NADP+ reductase [http://en.wikipedia.org/wiki/Ferredoxin—NADP(%2B)_reductase] is an enzyme that catalyzes the reduction of NADP+ to NADPH.  This enzyme belongs to a family of enzymes called oxidoreductases[http://en.wikipedia.org/wiki/Oxidoreductase] that contain iron-sulfur proteins as electron donors and NAD+ or NADP+ as electron acceptors. FAD, [flavin adenine dinucleotide][http://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide], is also a cofactor of FNR. The ferredoxin NADP+ reductase participates in a general reaction that proceeds as follows:
 reduced ferredoxin + NADP+  H  +  2 oxidized ferredoxin + NADPH
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 == Anaerobic Function ==
-	In many facultatively anaerobic bacteria, this protein acts as an oxygen sensor modifying gene expression that adapts the cell to anaerobic growth. The activity of FNR regulates the cells ability to metabolize aerobically or anaerobically so that when oxygen is abundant, FNR is destabilized and converted into an inactive form. The protein is activated when there are low oxygen tensions. This function is known as transcriptional sensor-regulation (link?). The predominant pathway in which this regulation occurs is through binding or oxidation-reduction of oxygen in the iron sulfur center, in which the iron serves as the initiating cofactor that interacts with the oxygen when it is abundant. This is a reversibly constitutive regulation pathway.
+	In many facultatively anaerobic bacteria, this protein acts as an oxygen sensor modifying gene expression that adapts the cell to anaerobic growth. The activity of FNR regulates the cells ability to metabolize aerobically or anaerobically so that when oxygen is abundant, FNR is destabilized and converted into an inactive form. The protein is activated when there are low oxygen tensions. This function is known as transcriptional sensor-regulation. The predominant pathway in which this regulation occurs is through binding or oxidation-reduction of oxygen in the iron sulfur center, in which the iron serves as the initiating cofactor that interacts with the oxygen when it is abundant. This is a reversibly constitutive regulation pathway.
 	In its active form, the protein is dimeric and contains a 4Fe-4S2+ cluster and when inactive, the protein is monomeric and containts a 3Fe-4S2+ cluster.