1.14.13.236: toluene 4-monooxygenase
This is an abbreviated version!
For detailed information about toluene 4-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.236
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1.14.13.236
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hydroxylase
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diiron
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mendocina
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p-cresol
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regiospecificity
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ferredoxins
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cepacia
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rieske
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synthesis
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pickettii
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ortho-monooxygenase
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m-nitrophenol
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nitrobenzene
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2-naphthol
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3-monooxygenase
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rieske-type
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four-protein
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diferric
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o-xylene
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norcarane
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xanthobacter
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analysis
- 1.14.13.236
- hydroxylase
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diiron
- mendocina
- p-cresol
-
regiospecificity
- ferredoxins
- cepacia
-
rieske
- synthesis
- pickettii
-
ortho-monooxygenase
- m-nitrophenol
- nitrobenzene
- 2-naphthol
-
3-monooxygenase
-
rieske-type
-
four-protein
-
diferric
- o-xylene
- norcarane
- xanthobacter
- analysis
Reaction
Synonyms
T4moD, T4moF, T4MOH, TMO, TmoA, TmoC, TmoF, toluene-4-monooxygenase system protein A, TOM, TomA3
ECTree
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Cofactor
Cofactor on EC 1.14.13.236 - toluene 4-monooxygenase
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Ferredoxin
ferredoxin binding leads to rearrangement of a loop about 30 A distal with a tightly matched, hydrogen bonded contact surface that places the [2Fe-2S] and diiron centres in their closest possible approach for electron transfer
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complexes with phenolic products yield an asymmetric my-phenoxo-bridged diiron center and a shift of diiron ligand E231 into a hydrogen bonding position with conserved residue T201
iron-sulfur centre
component contains a Rieske ferredoxin centre. H-bonding to the Rieske [2Fe-2S] center involves four (H47, Q48, A66, and H67 of T4MOC) of the five backbone amide H-bonds expected, the fifth backbone amide (I50 of T4MOC) fails to exhibit a hyperfine shift
iron-sulfur centre
component T4MOC contains a Rieske-type iron-sulfur center
iron-sulfur centre
study of the Fe(II)Fe(II) active site in the hydroxylase component of toluene-4 monoxygenase and the complex of T4moH bound by its effector protein, T4moD. Binding of the effector protein changes the geometry of one iron center and orientation of its redox active orbital to accommodate the binding of O2 in a bridged structure for efficient 2-electron transfer that can form a peroxo intermediate