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Literature summary for 1.12.99.6 extracted from

  • Beaton, S.E.; Evans, R.M.; Finney, A.J.; Lamont, C.M.; Armstrong, F.A.; Sargent, F.; Carr, S.B.
    The structure of hydrogenase-2 from Escherichia coli implications for H2-driven proton pumping (2018), Biochem. J., 475, 1353-1370 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.12.99.6

Cloned(Commentary)

Cloned (Comment) Organism
an overexpression system is described that facilitates the determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion technique, the crystal structure of recombinant enzyme is solved to a maximum resolution of 1.5 A (reduced) or 2.2 A (as-isolated) Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane periplasmic-facing membrane-bound complex Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2 + acceptor Escherichia coli the periplasmic-facing membrane-bound complex functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient reduced acceptor
-
 ?
H2 + acceptor Escherichia coli K12 the periplasmic-facing membrane-bound complex functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient reduced acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P69741
-
-
Escherichia coli K12 P69741
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + acceptor the periplasmic-facing membrane-bound complex functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient Escherichia coli reduced acceptor
-
 ?
H2 + acceptor the periplasmic-facing membrane-bound complex functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient Escherichia coli K12 reduced acceptor
-
 ?
H2 + oxidized benzyl viologen
-
 Escherichia coli H+ + reduceded benzyl viologen
-
 ?
H2 + oxidized benzyl viologen
-
 Escherichia coli K12 H+ + reduceded benzyl viologen
-
 ?

Subunits

Subunits Comment Organism
? the complex consists of a tightly bound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein (HybB) Escherichia coli

Synonyms

Synonyms Comment Organism
Hyd-2
-
 Escherichia coli
hydrogenase-2
-
 Escherichia coli

Expression

Organism Comment Expression
Escherichia coli present in cells at low levels during anaerobic respiration up

General Information

General Information Comment Organism
additional information HybO availability is an important limiting factor for native Hyd-2 synthesis Escherichia coli
physiological function the periplasmic-facing membrane-bound complex functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient. HybO availability is an important limiting factor for native Hyd-2 synthesis Escherichia coli