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Literature summary extracted from

  • Moebius, K.; Arias-Cartin, R.; Breckau, D.; Haennig, A.L.; Riedmann, K.; Biedendieck, R.; Schroeder, S.; Becher, D.; Magalon, A.; Moser, J.; Jahn, M.; Jahn, D.
    Heme biosynthesis is coupled to electron transport chains for energy generation (2010), Proc. Natl. Acad. Sci. USA, 107, 10436-10441.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.5.3 gene hemG, expression of His-tagged enzyme in Bacillus megaterium Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.3.5.3 additional information four electron transport chains from HemG via diverse quinones to cytochrome bo3, cytochrome bd, nitrate reductase, and fumarate reductase were reconstituted in vitro from purified components, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.5.3 0.0173
-
 menaquinone recombinant His-tagged enzyme, pH and temperature not specified in the publication Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.3 membrane associated Escherichia coli 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.5.3 150000
-
 recombinant enzyme, gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.3 protoporphyrinogen IX + 3 menaquinone Escherichia coli under anaerobic conditions protoporphyrin IX + 3 menaquinol
-
 ?
1.3.5.3 protoporphyrinogen IX + 3 ubiquinone Escherichia coli under aerobic conditions protoporphyrin IX + 3 ubiquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.3 Escherichia coli
-
 gene hemG
-
1.7.5.1 Escherichia coli
-
-
-
7.1.1.5 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.5.3 native enzyme solubilized from membranes by anion exchange chromatography, recombinant His-tagged enzyme from Bacillus megaterium byy affinity chromatography and gel filtration. Removal of the fused His-tag via protease digestion does not change the catalytic properties Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.5.3 0.0000042
-
 membrane associated enzyme with substrates protoporphyrinogen IX and triphenyltetrazolium chloride, pH and temperature not specified in the publication Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.3 additional information potential electron acceptors, i.e. 2, 6-dichloroindophenol, phenazine methosulfate, menadione, and vitamin K1, respectively, directly oxidize the substrate in the absence of HemG Escherichia coli ?
-
 ?
1.3.5.3 protoporphyrinogen IX + 3 menaquinone
-
 Escherichia coli protoporphyrin IX + 3 menaquinol
-
 ?
1.3.5.3 protoporphyrinogen IX + 3 menaquinone under anaerobic conditions Escherichia coli protoporphyrin IX + 3 menaquinol
-
 ?
1.3.5.3 protoporphyrinogen IX + 3 triphenyltetrazolium chloride artificial electron acceptor Escherichia coli protoporphyrin IX + ?
-
 ?
1.3.5.3 protoporphyrinogen IX + 3 ubiquinone
-
 Escherichia coli protoporphyrin IX + 3 ubiquinol
-
 ?
1.3.5.3 protoporphyrinogen IX + 3 ubiquinone under aerobic conditions Escherichia coli protoporphyrin IX + 3 ubiquinol
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.5.3 hexamer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.3.5.3 HemG
-
 Escherichia coli
1.3.5.3 PPO
-
 Escherichia coli
1.3.5.3 protoporphyrinogen IX oxidase
-
 Escherichia coli
1.7.5.1 NarG
-
 Escherichia coli
7.1.1.5 Cyd oxidase
-
 Escherichia coli
7.1.1.5 cytochrome bd oxidase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.3 FMN no direct electron transfer to a terminal oxidoreductase Escherichia coli

General Information

EC Number General Information Comment Organism
1.3.5.3 additional information detailed model of heme biosynthesis coupled energy generation, overview Escherichia coli
1.3.5.3 physiological function the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cytochrome bo3 , cytochrome bd, and nitrate reductase contribute to the proton motive force that drives ATP formation Escherichia coli
1.7.5.1 physiological function mutants deficient in all three nitrate reductases narGHI, narXYZ, napFDAGHCB are capable of sustaining 48% of protoporphyrinogen IX oxidases activity and 65% of wild-type activity, respectively Escherichia coli
7.1.1.5 metabolism the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cyo, Cyd and Nar contribute to the proton motive force that drives ATP formation. oxygen-dependent cytochrome oxidases, cytochrome bo3 (Cyo) and cytochrome bd (Cyd) oxidase, sustain up to 67% (Cyd) and 78% (Cyo) of HemG activity in the absence of ubiquinone, indicating a tight association of the quinones with the enzyme complexes during preparation Escherichia coli