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PDBsum entry 4z40
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Oxidoreductase
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PDB id
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4z40
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References listed in PDB file
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Key reference
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Title
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Structural basis of enzymatic benzene ring reduction.
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Authors
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T.Weinert,
S.G.Huwiler,
J.W.Kung,
S.Weidenweber,
P.Hellwig,
H.J.Stärk,
T.Biskup,
S.Weber,
J.J.Cotelesage,
G.N.George,
U.Ermler,
M.Boll.
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Ref.
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Nat Chem Biol, 2015,
11,
586-591.
[DOI no: ]
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PubMed id
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Abstract
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In chemical synthesis, the widely used Birch reduction of aromatic compounds to
cyclic dienes requires alkali metals in ammonia as extremely low-potential
electron donors. An analogous reaction is catalyzed by benzoyl-coenzyme A
reductases (BCRs) that have a key role in the globally important bacterial
degradation of aromatic compounds at anoxic sites. Because of the lack of
structural information, the catalytic mechanism of enzymatic benzene ring
reduction remained obscure. Here, we present the structural characterization of
a dearomatizing BCR containing an unprecedented tungsten cofactor that transfers
electrons to the benzene ring in an aprotic cavity. Substrate binding induces
proton transfer from the bulk solvent to the active site by expelling a Zn(2+)
that is crucial for active site encapsulation. Our results shed light on the
structural basis of an electron transfer process at the negative redox potential
limit in biology. They open the door for biological or biomimetic alternatives
to a basic chemical synthetic tool.
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