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  Structure of Xanthine Oxidase-Related 4-Hydroxybenzoyl-CoA Reductase with an Additional [4Fe-4S] Cluster and an Inverted Electron Flow

Unciuleac, M., Warkentin, E., Page, C. C., Boll, M., & Ermler, U. (2004). Structure of Xanthine Oxidase-Related 4-Hydroxybenzoyl-CoA Reductase with an Additional [4Fe-4S] Cluster and an Inverted Electron Flow. Structure, 12(12), 2249-2256. doi:10.1016/j.str.2004.10.008.

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 Creators:
Unciuleac, Mihaela1, Author
Warkentin, Eberhard2, Author           
Page, Christopher C.3, Author
Boll, Matthias1, Author
Ermler, Ulrich2, Author           
Affiliations:
1Institut für Biologie II, Mikrobiologie, 79104 Freiburg, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3The Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104 USA, ou_persistent22              

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 Abstract: The Mo-flavo-Fe/S-dependent heterohexameric protein complex 4-hydroxybenzoyl-CoA reductase (4-HBCR, dehydroxylating) is a central enzyme of the anaerobic degradation of phenolic compounds and belongs to the xanthine oxidase (XO) family of molybdenum enzymes. Its X-ray structure was established at 1.6 Å resolution. The most pronounced difference between 4-HBCR and other structurally characterized members of the XO family is the insertion of 40 amino acids within the β subunit, which carries an additional [4Fe-4S] cluster at a distance of 16.5 Å to the isoalloxazine ring of FAD. The architecture of 4-HBCR and concomitantly performed electron transfer rate calculations suggest an inverted electron transfer chain from the donor ferredoxin via the [4Fe-4S] cluster to the Mo over a distance of 55 Å. The binding site of 4-hydroxybenzoyl-CoA is located in an 18 Å long channel lined up by several aromatic side chains around the aromatic moiety, which are proposed to shield and stabilize the postulated radical intermediates during catalysis.

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Language(s): eng - English
 Dates: 2004-10-082004-03-192004-10-132004-12-072004-12-07
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.str.2004.10.008
PMID: 15576037
 Degree: -

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Title: Structure
  Other : Structure
Source Genre: Journal
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Publ. Info: London : Cell Press
Pages: - Volume / Issue: 12 (12) Sequence Number: - Start / End Page: 2249 - 2256 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1