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Issue 32, 2017
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Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies

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Abstract

Nature guides the flow of electrons in biological systems with the assistance of multi-heme proteins called cytochromes. In an effort to understand natures approach to developing electronic systems, three peptides that are compositionally identical but sequentially distinct have been designed to study the impact of morphology and hydrophobicity on heme coordination and function.

Graphical abstract: Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies

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Publication details

The article was received on 04 May 2017, accepted on 26 Jun 2017 and first published on 07 Aug 2017


Article type: Communication
DOI: 10.1039/C7OB01081H
Citation: Org. Biomol. Chem., 2017,15, 6725-6730
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    Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies

    H. Christopher Fry, A. R. Wood and L. A. Solomon, Org. Biomol. Chem., 2017, 15, 6725
    DOI: 10.1039/C7OB01081H

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