Published September 20, 2005
| Version Published
Journal Article
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Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires
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 mu M 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.
Additional Information
© 2005 by the National Academy of Sciences. Contributed by Harry B. Gray, July 27, 2005. Published online before print September 12, 2005, 10.1073/pnas.0506336102. This work was supported by National Institutes of Health Grants GM65011 (to S.M.C.), DK19038 and GM070868 (both to H.B.G.), and GM27659 (to D.M.D.) and Australian Research Council Grant DP0208320 (to H.C.F. and J.M.G.). Data deposition: The coordinates and structure factors of the complex have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 2BT3 [PDB]).Attached Files
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Additional details
Identifiers
- PMCID
- PMC1224652
- Eprint ID
- 2132
- Resolver ID
- CaltechAUTHORS:CONpnas05
Funding
- NIH
- GM65011
- NIH
- DK19038
- NIH
- GM070868
- Australian Research Council
- DP0208320
Dates
- Created
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2006-03-19Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field