Issue 18, 2007
From the journal:

Chemical Communications

Human frataxin: iron and ferrochelatase binding surface†

Krisztina Z. Bencze,a   Taejin Yoon,‡b   César Millán-Pacheco,c   Patrick B. Bradley,a   Nina Pastor,c   J. A. Cowanb  and  Timothy L. Stemmler*a  

* Corresponding authors

a Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, MI 49201, USA
E-mail: tstemmle@med.wayne.edu

b Department of Chemistry, Ohio State University, Columbus, OH 43210, USA

c Facultad de Ciencias, Universidad Autónoma del Estado de Morelos, Cuernavaca, Morelos, México

Abstract

The coordinated iron structure and ferrochelatase binding surface of human frataxin have been characterized to provide insight into the protein's ability to serve as the iron chaperone during heme biosynthesis.

Graphical abstract: Human frataxin: iron and ferrochelatase binding surface

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Article information

DOI
https://doi.org/10.1039/B703195E
Article type
Communication
Submitted
02 Mar 2007
Accepted
19 Mar 2007
First published
28 Mar 2007

Chem. Commun., 2007, 1798-1800

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Human frataxin: iron and ferrochelatase binding surface

K. Z. Bencze, T. Yoon, C. Millán-Pacheco, P. B. Bradley, N. Pastor, J. A. Cowan and T. L. Stemmler, Chem. Commun., 2007, 1798 DOI: 10.1039/B703195E

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