[Fe4S4] cubane in sulfite reductases: new insights into bonding properties and reactivity

Author:

Khan Shahriar N.1,Griffith Alexa2,De Proft Frank3ORCID,Miliordos Evangelos1,Havenith Remco W. A.45ORCID,Bykov Dmytro2,Cunha Ana V.236ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849-5312, USA

2. Center for Computational Sciences, Oak Ridge National Laboratory, Oak Ridge, TN 37831-6373, USA

3. Eenheid Algemene Chemie (ALGC), Vrije Universiteit Brussel (VUB), Pleinlaan 2, 1050 Brussels, Belgium

4. Stratingh Institute for Chemistry and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

5. Ghent Quantum Chemistry Group, Department of Chemistry, Ghent University, Krijgslaan 281 (S3), B-9000 Gent, Belgium

6. Department of Chemistry of the University of Antwerp, Groenenborgerlaan 171, 2020 Antwerp, Belgium

Abstract

The dissimilatory sulfite reductase enzyme has very characteristic active site where the substrate binds to an iron site, ligated by a siroheme macrocycle and a thiol directly connected to a [Fe4S4] cluster.

Funder

Office of Science

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

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