Subsystem: Pyruvate:ferredoxin oxidoreductase

This subsystem's description is:

In mitochondria and most aerobic bacteria, oxidative pyruvate decarboxylation, a central step in energy metabolism, is catalyzed by the pyruvate dehydrogenase multienzyme complex. In archaea, most anaerobic bacteria, and amitochondriate eukaryotes, this reaction is catalyzed reversibly by a single enzyme, pyruvate:ferredoxin oxidoreductase (PFOR), the electron acceptor being either ferredoxin or flavodoxin. The enzyme contains [4Fe-4S] clusters and thiamine pyrophosphate. In strictly anaerobic microorganisms PFOR is involved in substrate-level phosphorylation. In many nitrogen-fixing microorganisms, it is the source of low-potential electrons for nitrogenase, whereas in acetogenic bacteria like Clostridium thermoaceticum, it links glycolysis to the Wood–Ljungdahl pathway of acetyl-CoA synthesis.

In contrast to pyruvate dehydrogenase, PFOR can also catalyze the reverse reaction, i.e., the reductive carboxylation of acetyl-CoA provided that a sufficiently low-potential electron donor (like ferredoxin) is available. It has been reported for many obligatory anaerobes, including some photosynthetic bacteria, and more recently for an extremely thermophilic aerobic microorganism. This reverse reaction is important for some autotrophs because it serves to assimilate CO2 into cell carbon.

Hypothetical NADPH-dependent oxidoreductases tend to cluster with both types of PFOR, they are encoded in this SS as auxiliary roles (AUX).

For more information, please check out the description and the additional notes tabs, below

Literature ReferencesPyruvate ferredoxin oxidoreductase and its radical intermediate. Ragsdale SW Chemical reviews 2003 Jun12797832
Helicobacter pylori porCDAB and oorDABC genes encode distinct pyruvate:flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP. Hughes NJ Journal of bacteriology 1998 Mar9495749
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Taxonomy Pattern 
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Domain
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PFORaPFORbPFORdPFORyPFORePFORfPFORHyp1OxRed1OxRed2
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In mitochondria and most aerobic bacteria, oxidative pyruvate decarboxylation, a central step in energy metabolism, is catalyzed by the pyruvate dehydrogenase multienzyme complex. In archaea, most anaerobic bacteria, and amitochondriate eukaryotes, this reaction is catalyzed reversibly by a single enzyme, pyruvate:ferredoxin oxidoreductase (PFOR), the electron acceptor being either ferredoxin or flavodoxin. The enzyme contains [4Fe-4S] clusters and thiamine pyrophosphate. In strictly anaerobic microorganisms PFOR is involved in substrate-level phosphorylation. In many nitrogen-fixing microorganisms, it is the source of low-potential electrons for nitrogenase, whereas in acetogenic bacteria like Clostridium thermoaceticum, it links glycolysis to the Wood–Ljungdahl pathway of acetyl-CoA synthesis.

In contrast to pyruvate dehydrogenase, PFOR can also catalyze the reverse reaction, i.e., the reductive carboxylation of acetyl-CoA provided that a sufficiently low-potential electron donor (like ferredoxin) is available. It has been reported for many obligatory anaerobes, including some photosynthetic bacteria, and more recently for an extremely thermophilic aerobic microorganism. This reverse reaction is important for some autotrophs because it serves to assimilate CO2 into cell carbon.

Hypothetical NADPH-dependent oxidoreductases tend to cluster with both types of PFOR, they are encoded in this SS as auxiliary roles (AUX).
References:

1. Ragsdale SW. 2003. Pyruvate ferredoxin oxidoreductase and its radical intermediate. Chem Rev, 103(6):2333-46. Review. PMID: 12797832

2. Ikeda et al., 2006. Anabolic five subunit-type pyruvate:ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6. Biochemical and Biophysical Research Communications 340 (2006) 76–82

2. Chabriere et al. 1999. Crystal structuresofthe key anaerobic enzyme pyruvate:ferredoxinoxidoreductase, free and in complex with pyruvate. Nature Structural Biology, 6:182-190

3. KLETZIN and ADAMS. 1996. Molecular and Phylogenetic Characterization of Pyruvate and 2-Ketoisovalerate Ferredoxin Oxidoreductases from Pyrococcus furiosus and Pyruvate Ferredoxin Oxidoreductase from Thermotoga maritima. J.Bact, 178:248–257

Currently selected organism: Escherichia coli 2731150 (open scenarios overview page for organism)