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Literature summary for 1.5.7.2 extracted from

  • Schut, G.; Zadvornyy, O.; Wu, C.; Peters, J.; Boyd, E.; Adams, M.
    The role of geochemistry and energetics in the evolution of modern respiratory complexes from a proton-reducing ancestor (2016), Biochim. Biophys. Acta, 1857, 958-970 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic tree Methanosarcina mazei
phylogenetic tree Methanothrix thermoacetophila

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Methanosarcina mazei 16020
-
membrane
-
Methanothrix thermoacetophila 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methanophenazine + reduced F420 + 2 H+ Methanosarcina mazei
-
reduced methanophenazine + oxidized F420
-
?
methanophenazine + reduced ferredoxin + 2 H+ Methanothrix thermoacetophila
-
reduced methanophenazine + oxidized ferredoxin
-
?

Organism

Organism UniProt Comment Textmining
Methanosarcina mazei
-
-
-
Methanothrix thermoacetophila
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methanophenazine + reduced F420 + 2 H+
-
Methanosarcina mazei reduced methanophenazine + oxidized F420
-
?
methanophenazine + reduced ferredoxin + 2 H+
-
Methanothrix thermoacetophila reduced methanophenazine + oxidized ferredoxin
-
?

Synonyms

Synonyms Comment Organism
cofactor F420-dependent FPO
-
Methanosarcina mazei
F420H2:phenazine oxidoreductase
-
Methanosarcina mazei
F420H2:phenazine oxidoreductase
-
Methanothrix thermoacetophila
Fd-dependent FPO
-
Methanothrix thermoacetophila
ferredoxin-dependent FPO
-
Methanothrix thermoacetophila
FPOC
-
Methanosarcina mazei
FPOF
-
Methanothrix thermoacetophila

General Information

General Information Comment Organism
evolution evolutionary trajectory of these oxidoreductases from a proton-reducing ancestral respiratory complex (ARC), overview. The diversification of ARC to membrane-bound hydrogenase (MBH), archaeal respiratory complex (MBX), FPO and eventually NADH quinone oxidoreductase (NUO) was driven by the larger energy yields associated with coupling ferredoxin oxidation to the reduction of oxidants with increasing electrochemical potential, including protons, SĀ° and membrane soluble organic compounds such as phenazines and quinone derivatives. Phylogenetic tree. Homology between the subunits of FPOF and FPOC with those in MBX and MBH. Evolution of FPO, detailed overview. FPO is now present only in strictly anaerobic, acetate-utilizing and sulfate-reducing archaea Methanosarcina mazei
evolution evolutionary trajectory of these oxidoreductases from a proton-reducing ancestral respiratory complex (ARC), overview. The diversification of ARC to membrane-bound hydrogenase (MBH), archaeal respiratory complex (MBX), FPO and eventually NADH quinone oxidoreductase (NUO) was driven by the larger energy yields associated with coupling ferredoxin oxidation to the reduction of oxidants with increasing electrochemical potential, including protons, SĀ° and membrane soluble organic compounds such as phenazines and quinone derivatives. Phylogenetic tree. Homology between the subunits of FPOF and FPOC with those in MBX and MBH. Evolution of FPO, detailed overview. FPO is now present only in strictly anaerobic, acetate-utilizing and sulfate-reducing archaea Methanothrix thermoacetophila
additional information FPO demonstrates the flexible nature of the ARC-related complexes with respect to electron input and energetics reflected by differences in redox carriers and number of ions translocated Methanosarcina mazei
additional information FPO demonstrates the flexible nature of the ARC-related complexes with respect to electron input and energetics reflected by differences in redox carriers and number of ions translocated Methanothrix thermoacetophila
physiological function the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420 Methanosarcina mazei
physiological function the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420. The FPO complex is mainly found in acetate-utilizing, methane-producing anaerobic Archaea where it functions to reduce the membrane-associated cofactor methanophenazine using either ferredoxin or the cytoplasmic cofactor F420 Methanothrix thermoacetophila