Conjugates of Heme-Thiolate Enzymes with Photoactive Metal-Diimine Wires
Abstract
Heme-thiolate enzymes, notably cytochromes P450 and nitric oxide synthases, use dioxygen to oxygenatesubstrates. Photoactive metal-diimine molecular wires that are capable of effecting rapid redox state changesat buried active sites have been developed to generate intermediates in the catalytic cycles of these enzymes.Wires that feature a photoactive head group tethered to an active-site ligand bind P450CAM and induciblenitric oxide synthase (iNOS) primarily by hydrophobic interactions. The wire-binding specificity of eachenzyme is critically dependent on the structural flexibility of the protein. P450CAM:wire conjugates canadopt open or partially open conformations, thereby accommodating a wide range of wires, whereas onlylong wires with smaller [Re(CO)_3(bpy)Im]^+ head groupsare able to bind tightly in the rigid active-site channel of iNOS. Dansyl-terminated molecular wires functionas highly sensitive and isoform specific fluorescent sensors for P450CAM.
Additional Information
© Springer-Verlag Berlin Heidelberg 2006. Figure 11 was adopted from a version prepared by Alex Dunn. We thank him and others in the Caltech molecular wires group (Ivan Dmochowski, Jon Wilker, Corinna Hess, Wendy Belliston-Bittner, Nick Halpern-Manners) for contributions that are summarized in this chapter. Our work is supported by NIH, NSF, the Ellison Medical Foundation Senior Scholar Award in Aging (to HBG), and the Arnold and Mabel Beckman Foundation.Additional details
- Eprint ID
- 98304
- Resolver ID
- CaltechAUTHORS:20190828-102318186
- NIH
- NSF
- Ellison Medical Foundation
- Arnold and Mabel Beckman Foundation
- Created
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2019-08-28Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field
- Series Name
- Structure and Bonding
- Series Volume or Issue Number
- 123