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Journal:JBIC:22

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The crystal structure of AoCO4 demonstrated that mono-oxygenase and diphenolase reactivity cannot be explained by accessibility to copper ions. Based on the observations that CuA is restricted by a Phe residue in plant catechol oxidases, but not in tyrosinases, it has been suggested that o-diphenols bind to CuB, whereas monophenols bind to CuA. However, both copper ions were solvent-exposed and accessible to substrates in AoCO4.
The crystal structure of AoCO4 demonstrated that mono-oxygenase and diphenolase reactivity cannot be explained by accessibility to copper ions. Based on the observations that CuA is restricted by a Phe residue in plant catechol oxidases, but not in tyrosinases, it has been suggested that o-diphenols bind to CuB, whereas monophenols bind to CuA. However, both copper ions were solvent-exposed and accessible to substrates in AoCO4.
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The crystal structure of the full-length AoCO4 revealed an elongated electron density between CuA and CuB in the catalytic centre. This was best refined as a diatomic oxygen moiety. The O2 atom of the dioxygen moiety was approximately 2.0 Å and 2.3 Å away from CuA and CuB, respectively, and the O1 atom of dioxygen moiety was 2.6 Å away from each copper ion. Furthermore, the UV/VIS absorption spectrum indicated that enzyme exists partially in the oxy-form, because native form as isolated exhibited a clear absorption band at 350 nm.
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The crystal structure of the full-length AoCO4 revealed an elongated electron density between CuA and CuB in the catalytic centre. This was best refined as a <scene name='55/559101/Cv/4'>diatomic oxygen moiety</scene>. The O2 atom of the dioxygen moiety was approximately 2.0 Å and 2.3 Å away from CuA and CuB, respectively, and the O1 atom of dioxygen moiety was 2.6 Å away from each copper ion. Furthermore, the UV/VIS absorption spectrum indicated that enzyme exists partially in the oxy-form, because native form as isolated exhibited a clear absorption band at 350 nm.
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Revision as of 10:34, 17 September 2013

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