Can beta sheets bind multiple heme cofactors?

Published in Chemistry
Can beta sheets bind multiple heme cofactors?

Share this post

Choose a social network to share with, or copy the shortened URL to share elsewhere

This is a representation of how your post may appear on social media. The actual post will vary between social networks

This research work is an extension of our previous successes on designing heme binding multi-stranded beta sheet mini-proteins. Heme-proteins form an essential part of several biological reactions, such as oxidation-reduction, electron transfer, energy harvesting, and gaseous exchange. Therefore, designing mini proteins (<50 amino acids) that can encapsulate the features of these complex proteins would have great applications in developing new catalysts and novel functions.

The ultimate goal of our work is to design multi-heme protein conduits. In nature, protein conduits like the cytochromes contain several heme groups coupled together to facilitate an efficient electron transport and enzymatic activity. Inspired by this, several groups have attempted to create the common coiled-coil motif by designing multi-heme alpha-helical proteins. In contrast, there are lesser known naturally occurring heme binding β-sheet proteins. Beta-sheet design also presents challenges due to aggregation and insolubility in aqueous solutions.

Here, we demonstrate the design of multi-stranded beta-sheet mini-proteins that are able to coordinate di and tetra heme with high affinities. These beta-sheet mini-proteins can attach in a versatile orientation either by stacking or sidewise mimicking naturally occuring multi-heme protein conduits. 

The research article, published in Communications Chemistry, can be downloaded from here:

Please sign in or register for FREE

If you are a registered user on Research Communities by Springer Nature, please sign in

Subscribe to the Topic

Physical Sciences > Chemistry

Related Collections

With collections, you can get published faster and increase your visibility.

Plasmon-mediated chemistry

This collection aims to cover a comprehensive range of topics related to plasmon-mediated chemical reactions.

Publishing Model: Open Access

Deadline: Jan 31, 2024

Coacervation in systems chemistry

This Guest Edited Collection aims to bring together research at the intersection of systems chemistry and coacervation. We welcome both experimental and theoretical studies.

Publishing Model: Open Access

Deadline: Dec 31, 2023