Conjugates of heme-thiolate enzymes with photoactive metal-diimine wires

Stephen M. Contakes, Yen Hoang Le Nguyen, Harry B. Gray, Edith C. Glazer, Anna Maria Hays, David B. Goodin

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

4 Scopus citations


Heme-thiolate enzymes, notably cytochromes P450 and nitric oxide synthases, use dioxygen to oxygenate substrates. Photoactive metal-diimine molecular wires that are capable of effecting rapid redox state changes at 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 inducible nitric oxide synthase (iNOS) primarily by hydrophobic interactions. The wirebinding specificity of each enzyme is critically dependent on the structural flexibility of the protein. P450CAM:wire conjugates can adopt open or partially open conformations, thereby accommodating a wide range of wires, whereas only long wires with smaller [Re(CO) 3(bpy)Im]+ head groups are able to bind tightly in the rigid active-site channel of iNOS. Dansyl-terminated molecular wires function as highly sensitive and isoform specific fluorescent sensors for P450CAM.

Original languageEnglish
Title of host publicationPhotofunctional Transition Metal Complexes
EditorsMichael Mingos, Vivian Yam, Peter Day, Xue Duan, Thomas Meyer, Gerard Parkin, Herbert Roesky, Jean-Piere Sauvage
Number of pages27
StatePublished - Jun 22 2007

Publication series

NameStructure and Bonding
ISSN (Print)0081-5993
ISSN (Electronic)1616-8550


  • Cytochromes P450
  • Electron transfer
  • Molecular wires
  • Nitric oxide synthase
  • Photochemistry

ASJC Scopus subject areas

  • Spectroscopy
  • Physical and Theoretical Chemistry
  • Inorganic Chemistry


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