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Media type:
E-Article
Title:
Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase
Contributor:
McCarthy, Erin L.;
Booker, Squire J.
imprint:
American Association for the Advancement of Science (AAAS), 2017
Published in:Science
Language:
English
DOI:
10.1126/science.aan4574
ISSN:
0036-8075;
1095-9203
Origination:
Footnote:
Description:
<jats:title>Refueling an enzyme</jats:title>
<jats:p>
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
<jats:italic>Escherichia coli</jats:italic>
, 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.
</jats:p>
<jats:p>
<jats:italic>Science</jats:italic>
, this issue p.
<jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6361" page="373" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan4574">373</jats:related-article>
; see also p.
<jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6361" page="307" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aap9299">307</jats:related-article>
</jats:p>