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PDBsum entry 1v9q
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Oxygen storage/transport
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PDB id
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1v9q
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References listed in PDB file
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Key reference
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Title
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Coordinated design of cofactor and active site structures in development of new protein catalysts.
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Authors
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T.Ueno,
T.Koshiyama,
M.Ohashi,
K.Kondo,
M.Kono,
A.Suzuki,
T.Yamane,
Y.Watanabe.
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Ref.
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J Am Chem Soc, 2005,
127,
6556-6562.
[DOI no: ]
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PubMed id
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Abstract
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New methods for the synthesis of artificial metalloenzymes are important for the
construction of novel biocatalysts and biomaterials. Recently, we reported new
methodology for the synthesis of artificial metalloenzymes by reconstituting
apo-myoglobin with metal complexes (Ohashi, M. et al., Angew Chem., Int. Ed.
2003, 42, 1005-1008). However, it has been difficult to improve their
reactivity, since their crystal structures were not available. In this article,
we report the crystal structures of M(III)(Schiff base).apo-A71GMbs (M = Cr and
Mn). The structures suggest that the position of the metal complex in apo-Mb is
regulated by (i) noncovalent interaction between the ligand and surrounding
peptides and (ii) the ligation of the metal ion to proximal histidine (His93).
In addition, it is proposed that specific interactions of Ile107 with 3- and
3'-substituent groups on the salen ligand control the location of the Schiff
base ligand in the active site. On the basis of these results, we have
successfully controlled the enantioselectivity in the sulfoxidation of
thioanisole by changing the size of substituents at the 3 and 3' positions. This
is the first example of an enantioselective enzymatic reaction regulated by the
design of metal complex in the protein active site.
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