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Literature summary for 1.1.2.10 extracted from

  • Kalimuthu, P.; Daumann, L.J.; Pol, A.; Op den Camp, H.J.M.; Bernhardt, P.V.
    Electrocatalysis of a europium-dependent bacterial methanol dehydrogenase with its physiological electron-acceptor cytochrome cGJ (2019), Chemistry, 25, 8760-8768 .
    View publication on PubMed
Search for more literature for 1.1.2.10

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Methylacidiphilum fumariolicum

Metals/Ions

Metals/Ions Comment Organism Structure
Eu3+ the enzyme is dependent on the lanthanide europium Methylacidiphilum fumariolicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methanol + 2 cytochrome cGJ Methylacidiphilum fumariolicum
-
 formaldehyde + 2 reduced cytochrome cGJ
-
 r
methanol + 2 cytochrome cGJ Methylacidiphilum fumariolicum SolV
-
 formaldehyde + 2 reduced cytochrome cGJ
-
 r

Organism

Organism UniProt Comment Textmining
Methylacidiphilum fumariolicum
-
-
-
Methylacidiphilum fumariolicum SolV
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methanol + 2 cytochrome cGJ
-
 Methylacidiphilum fumariolicum formaldehyde + 2 reduced cytochrome cGJ
-
 r
methanol + 2 cytochrome cGJ electrochemic reaction, use of a Au/MU electrode for the electrontransfer process. The attenuation coefficient of DCPIP is known to be very sensitive to changes in pH, reactions with DCPIP are monitored at 600 nm Methylacidiphilum fumariolicum formaldehyde + 2 reduced cytochrome cGJ
-
 r
methanol + 2 cytochrome cGJ
-
 Methylacidiphilum fumariolicum SolV formaldehyde + 2 reduced cytochrome cGJ
-
 r
methanol + 2 cytochrome cGJ electrochemic reaction, use of a Au/MU electrode for the electrontransfer process. The attenuation coefficient of DCPIP is known to be very sensitive to changes in pH, reactions with DCPIP are monitored at 600 nm Methylacidiphilum fumariolicum SolV formaldehyde + 2 reduced cytochrome cGJ
-
 r

Synonyms

Synonyms Comment Organism
Eu-MDH
-
 Methylacidiphilum fumariolicum
lanthanoid-dependent methanol dehydrogenase
-
 Methylacidiphilum fumariolicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 assay at Methylacidiphilum fumariolicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
 Methylacidiphilum fumariolicum

Cofactor

Cofactor Comment Organism Structure
2,7,9-tricarboxypyrroloquinoline quinone Eu-MDH harbours a redox active 2,7,9-tricarboxypyrroloquinoline quinone (PQQ) cofactor which is non-covalently bound but coordinates trivalent lanthanoid elements including Eu3+ Methylacidiphilum fumariolicum
cytochrome cGJ
-
 Methylacidiphilum fumariolicum

General Information

General Information Comment Organism
physiological function lanthanoid-dependent methanol dehydrogenase (Eu-MDH) from the acidophilic verrucomicrobial methanotroph Methylacidiphilum fumariolicum SolV has its own physiological cytochrome cGJ electron acceptor. Eu-MDH harbours a redox active 2,7,9-tricarboxypyrroloquinoline quinone (PQQ) cofactor which is non-covalently bound but coordinates trivalent lanthanoid elements including Eu3+. Eu-MDH and the cytochrome are co-adsorbed with the biopolymer chitosan and cast onto a mercaptoundecanol (MU) monolayer modified Au working electrode. Cyclic voltammetry of cytochrome cGJ reveals a well-defined quasi-reversible FeIII/II redox couple at +255 mV versus normal hydrogen electrode (NHE) at pH 7.5, and this response is pH independent. The reversible one-electron response of the cytochrome cGJ transforms into a sigmoidal catalytic wave in the presence of Eu-MDH and its substrates (methanol or formaldehyde). The catalytic current is pH-dependent, and pH 7.3 is optimal Methylacidiphilum fumariolicum