De novo design of a single-chain diphenylporphyrin metalloprotein.

Journal Article (Journal Article)

We describe the computational design of a single-chain four-helix bundle that noncovalently self-assembles with fully synthetic non-natural porphyrin cofactors. With this strategy, both the electronic structure of the cofactor as well as its protein environment may be varied to explore and modulate the functional and photophysical properties of the assembly. Solution characterization (NMR, UV-vis) of the protein showed that it bound with high specificity to the desired cofactors, suggesting that a uniquely structured protein and well-defined site had indeed been created. This provides a genetically expressed single-chain protein scaffold that will allow highly facile, flexible, and asymmetric variations to enable selective incorporation of different cofactors, surface-immobilization, and introduction of spectroscopic probes.

Full Text

Duke Authors

Cited Authors

  • Bender, GM; Lehmann, A; Zou, H; Cheng, H; Fry, HC; Engel, D; Therien, MJ; Blasie, JK; Roder, H; Saven, JG; DeGrado, WF

Published Date

  • September 2007

Published In

Volume / Issue

  • 129 / 35

Start / End Page

  • 10732 - 10740

PubMed ID

  • 17691729

Pubmed Central ID

  • PMC2542652

Electronic International Standard Serial Number (EISSN)

  • 1520-5126

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja071199j


  • eng