Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase-Reference-Cited by-同舟云学术

Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase

Published:2017-10-20 Issue:6361 Volume:358 Page:373-377
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

McCarthy Erin L.¹^ORCID,Booker Squire J.¹²³^ORCID

Affiliation:

1. Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.

2. Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.

3. Howard Hughes Medical Institute, Pennsylvania State University, University Park, PA 16802, USA.

Abstract

Refueling an enzyme Lipoic acid is an eight-carbon fatty acid in which sulfur groups are appended on two carbon atoms by the enzyme lipoyl synthase (LipA). LipA provides the sulfurs from an auxiliary [4Fe-4S] cluster. McCarthy and Booker show that in Escherichia coli , the auxiliary LipA cluster is reconstituted by the iron-sulfur cluster carrier protein NfuA (see the Perspective by Rosenzweig). This occurs fast enough that LipA can act catalytically in the final step of lipoic acid biosynthesis. Science , this issue p. 373 ; see also p. 307

Funder

National Science Foundation

National Institute of General Medical Sciences

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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