Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires |
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| Authors: | Contakes Stephen M Juda Gregory A Langley David B Halpern-Manners Nicholas W Duff Anthony P Dunn Alexander R Gray Harry B Dooley David M Guss J Mitchell Freeman Hans C |
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| Affiliation: | Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA. |
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| Abstract: | Molecular wires comprising a Ru(II)- or Re(I)-complex head group, an aromatic tail group, and an alkane linker reversibly inhibit the activity of the copper amine oxidase from Arthrobacter globiformis (AGAO), with K(i) values between 6 muM and 37 nM. In the crystal structure of a Ru(II)-wire:AGAO conjugate, the wire occupies the AGAO active-site substrate access channel, the trihydroxyphenylalanine quinone cofactor is ordered in the "off-Cu" position with its reactive carbonyl oriented toward the inhibitor, and the "gate" residue, Tyr-296, is in the "open" position. Head groups, tail-group substituents, and linker lengths all influence wire-binding interactions with the enzyme. |
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