Issue 32, 2017

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

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

Supplementary files

Article information

Article type
Communication
Submitted
04 Maijs 2017
Accepted
26 Jūn. 2017
First published
07 Aug. 2017

Org. Biomol. Chem., 2017,15, 6725-6730

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements