ArticleMethods in enzymology2025
De novo design of four-helix bundle proteins to bind metalloporphyrin cofactors.
Article in Methods in enzymology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Less is more: miniaturized heme enzymes with broad reactivity.Chemical science · 2026Review
- Near-Infrared Fluorescence Imaging and Photothermal Therapy of Tumors Using a Targeted Helical Protein Scaffold.ACS applied bio materials · 2026Article
- Highly Stable Mn(V)-Nitrido and Nitrogen-Atom Transfer Reactivity within aJournal of the American Chemical Society · 2026Article
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Authors and funding
3 authors.
Funding
Abstract
The versatility of heme proteins in nature stems from the intricate control exerted by their protein scaffolds. De novo protein design offers a powerful means to dissect and recreate these structure-function relationships, enabling construction of novel metalloproteins with tailored functionalities. Here, we describe the computational design and characterization MPP1, a four-helix bundle protein designed to bind an abiological Mn-diphenylporphyrin (MnDPP) cofactor. Using parameterized coiled-coil backbones, flexible backbone sequence design in Rosetta, and structure-guided loop building, MPP1 was designed to accommodate the cofactor with precise positioning of axial ligands and second-shell interactions, as well as purposeful accessibility for oxidants and substrates. The resulting protein was the first crystallographically characterized de novo designed porphyrin-binding protein. MPP1 demonstrated the ability to stabilize a high-valent Mn(V)-oxo species and mediate thioether oxidation. This chapter details the computational strategies, cofactor incorporation, and solution characterization necessary to design and evaluate four-helix bundle proteins capable of binding porphyrin and porphyrin-like cofactors with atomic-level precision. Keywords: de novo design, protein design, bioinorganic chemistry, metalloporphyrins, heme proteins.
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