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Literature summary for 1.14.13.25 extracted from

  • Schwartz, J.K.; Wei, P.P.; Mitchell, K.H.; Fox, B.G.; Solomon, E.I.
    Geometric and electronic structure studies of the binuclear nonheme ferrous active site of toluene-4-monooxygenase: parallels with methane monooxygenase and insight into the role of the effector proteins in O2 activation (2008), J. Am. Chem. Soc., 130, 7098-7109.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron in MmoH Fe-water distances vary from about 1.9 to 2.7 A, showing Fe1 to be 5 or 6 coordinate. The effect of binding toluene-4-monooxygenase D/MmoB to toluene-4-monooxygenase H/MmoH is not to remove a water ligand from either iron but to induce a change in orientation of the terminal glutamate on Fe2. This allows O2 to bridge the diiron site and aligns the redox active orbital on each Fe for efficient 2-electron transfer, facilitating the formation of a stabilized peroxo intermediate synthetic construct

Organism

Organism UniProt Comment Textmining
synthetic construct
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Synonyms

Synonyms Comment Organism
MMOB
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synthetic construct
MMOH
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synthetic construct
sMMO
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synthetic construct
soluble methane monooxygenase
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synthetic construct