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PDBsum entry 2cfd
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Oxidoreductase
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PDB id
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2cfd
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References listed in PDB file
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Key reference
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Title
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Enantiomer-Specific binding of ruthenium(ii) molecular wires by the amine oxidase of arthrobacter globiformis.
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Authors
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D.B.Langley,
D.E.Brown,
L.E.Cheruzel,
S.M.Contakes,
A.P.Duff,
K.M.Hilmer,
D.M.Dooley,
H.B.Gray,
J.M.Guss,
H.C.Freeman.
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Ref.
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J Am Chem Soc, 2008,
130,
8069-8078.
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PubMed id
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Abstract
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The copper amine oxidase from Arthrobacter globiformis (AGAO) is reversibly
inhibited by molecular wires comprising a Ru(II) complex head group and an
aromatic tail group joined by an alkane linker. The crystal structures of a
series of Ru(II)-wire-AGAO complexes differing with respect to the length of the
alkane linker have been determined. All wires lie in the AGAO active-site
channel, with their aromatic tail group in contact with the
trihydroxyphenylalanine quinone (TPQ) cofactor of the enzyme. The TPQ cofactor
is consistently in its active ("off-Cu") conformation, and the side chain of the
so-called "gate" residue Tyr296 is consistently in the "gate-open" conformation.
Among the wires tested, the most stable complex is produced when the wire has a
-(CH2)4- linker. In this complex, the Ru(II)(phen)(bpy)2 head group is level
with the protein molecular surface. Crystal structures of AGAO in complex with
optically pure forms of the C4 wire show that the linker and head group in the
two enantiomers occupy slightly different positions in the active-site channel.
Both the Lambda and Delta isomers are effective competitive inhibitors of amine
oxidation. Remarkably, inhibition by the C4 wire shows a high degree of
selectivity for AGAO in comparison with other copper-containing amine oxidases.
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