Duplications of an iron–sulphur tripeptide leads to the formation of a protoferredoxin-Reference-Cited by-同舟云学术

Duplications of an iron–sulphur tripeptide leads to the formation of a protoferredoxin

Published:2016 Issue:92 Volume:52 Page:13456-13459
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Scintilla Simone¹²³⁴,Bonfio Claudia¹²³⁴,Belmonte Luca¹²³⁴,Forlin Michele¹²³⁴,Rossetto Daniele¹²³⁴,Li Jingwei⁵⁶⁷⁸,Cowan James A.⁵⁶⁷⁸,Galliani Angela⁹¹⁰¹¹⁴,Arnesano Fabio⁹¹⁰¹¹⁴,Assfalg Michael¹²¹³¹⁴⁴,Mansy Sheref S.¹²³⁴^ORCID

Affiliation:

1. CIBIO

2. University of Trento

3. 38123 Povo

4. Italy

5. Department of Chemistry and Biochemistry

6. The Ohio State University

7. Columbus

8. USA

9. Department of Chemistry

10. University of “Bari A. Moro”

11. 70125 Bari

12. Department of Biotechnology

13. University of Verona

14. 37134 Verona

Abstract

Based on UV-Vis, NMR, and EPR spectroscopies and DFT and molecular dynamics calculations, a model prebiotic [2Fe–2S] tripeptide was shown to accept and donate electrons.

Funder

Giovanni Armenise-Harvard Foundation

Simons Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CC/C6CC07912A

Reference26 articles.

1. Synthetic Analogues of the Active Sites of Iron−Sulfur Proteins

2. Discovering the electronic circuit diagram of life: structural relationships among transition metal binding sites in oxidoreductases

3. History of biological metal utilization inferred through phylogenomic analysis of protein structures

4. Determination of Nonligand Amino Acids Critical to [4Fe-4S]2+/+ Assembly in Ferredoxin Maquettes

5. Evolutionary history of redox metal-binding domains across the tree of life

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