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PDBsum entry 2bhf
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Oxidoreductase
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PDB id
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2bhf
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References listed in PDB file
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Key reference
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Title
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Dioxygen reduction by multi-Copper oxidases; a structural perspective.
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Authors
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I.Bento,
L.O.Martins,
G.Gato lopes,
M.Arménia carrondo,
P.F.Lindley.
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Ref.
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Dalton Trans, 2005,
21,
3507-3513.
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PubMed id
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Abstract
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The multi-copper oxidases oxidise substrate molecules by accepting electrons at
a mononuclear copper centre and transferring them to a trinuclear centre.
Dioxygen binds to the trinuclear centre and, following the transfer of four
electrons, is reduced to two molecules of water. The precise mechanism of this
reduction has been unclear, but recent X-ray structural studies using the CotA
endospore coat protein from Bacillus subtilis have given further insights into
the principal stages. It is proposed that the mechanism involves binding of the
dioxygen into the trinuclear centre so that it is sited approximately
symmetrically between the two type 3 copper ions with one oxygen atom close to
the type 2 copper ion. Further stages involve the formation of a peroxide
intermediate and following the splitting of this intermediate, the migration of
the hydroxide moieties towards the solvent exit channel. The migration steps are
likely to involve a movement of the type 2 copper ion and its environment.
Details of a putative mechanism are described herein based both on structures
already reported in the literature and on structures of the CotA protein in the
oxidised and reduced states and with the addition of peroxide and the inhibitor,
azide.
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