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Literature summary for 1.14.18.3 extracted from

  • Tumanova, L.V.; Tukhvatullin, I.A.; Burbaev, D.S.; Gvozdev, R.I.; Andersson, K.K.
    The binuclear iron site of membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M) (2008), Russ. J. Bioorg. Chem., 34, 177-185.
No PubMed abstract available
Search for more literature for 1.14.18.3

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Methylococcus capsulatus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ Cu2+ is involved in the active site of pMMOH Methylococcus capsulatus
Fe pMMOH bears a binuclear iron valence site [Fe(III)-Fe(IV)] Methylococcus capsulatus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
 1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH Methylococcus capsulatus
27000
-
 1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH Methylococcus capsulatus
47000
-
 1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH Methylococcus capsulatus
99000
-
 SDS-PAGE Methylococcus capsulatus

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
-
-
Methylococcus capsulatus M
-
-
-

Purification (Commentary)

Purification (Comment) Organism
FPLC liquid chromatography and Mono Q HR 5/50 GL column chromatography Methylococcus capsulatus

Subunits

Subunits Comment Organism
heterotrimer 1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
pMMO consists of two protein components: NADH oxidoreductase (pMMOR) and hydroxylase (pMMOH) Methylococcus capsulatus
sMMO consists of three components: hydroxylase (sMMOH), NADH-dependent reductase (sMMOR), and the regulatory protein B (sMMOB) Methylococcus capsulatus