The Alternative Route to Heme in the Methanogenic Archaeon Methanosarcina barkeri

In living organisms heme is formed from the common precursor uroporphyrinogen III by either one of two substantially different pathways. In contrast to eukaryotes and most bacteria which employ the so-called “classical” heme biosynthesis pathway, the archaea use an alternative route. In this pathway...

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Published in:Archaea 2014-01, Vol.2014 (2014), p.58-70
Main Authors: Kühner, Melanie, Haufschildt, Kristin, Neumann, Alexander, Storbeck, Sonja, Streif, Judith, Layer, Gunhild
Format: Article
Language:English
Subjects:
Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Bacteria
Biosynthesis
Biosynthetic Pathways - genetics
Enzymes
Genetic aspects
Genomes
Heme
Heme - biosynthesis
Methanobacteriaceae
Methanosarcina barkeri - enzymology
Methanosarcina barkeri - genetics
Methanosarcina barkeri - metabolism
Microbiological synthesis
Properties
Protein Multimerization
Proteins
Retention
Uroporphyrinogens - metabolism
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cited_by cdi_FETCH-LOGICAL-a563t-5d3c7d31e081fd0574624db31f88c1cd59d84e16aff2b3d5653f3a6ed62df983
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container_issue 2014
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container_title Archaea
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creator Kühner, Melanie
Haufschildt, Kristin
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Storbeck, Sonja
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Layer, Gunhild
description In living organisms heme is formed from the common precursor uroporphyrinogen III by either one of two substantially different pathways. In contrast to eukaryotes and most bacteria which employ the so-called “classical” heme biosynthesis pathway, the archaea use an alternative route. In this pathway, heme is formed from uroporphyrinogen III via the intermediates precorrin-2, sirohydrochlorin, siroheme, 12,18-didecarboxysiroheme, and iron-coproporphyrin III. In this study the heme biosynthesis proteins AhbAB, AhbC, and AhbD from Methanosarcina barkeri were functionally characterized. Using an in vivo enzyme activity assay it was shown that AhbA and AhbB (Mbar_A1459 and Mbar_A1460) together catalyze the conversion of siroheme into 12,18-didecarboxysiroheme. The two proteins form a heterodimeric complex which might be subject to feedback regulation by the pathway end-product heme. Further, AhbC (Mbar_A1793) was shown to catalyze the formation of iron-coproporphyrin III in vivo. Finally, recombinant AhbD (Mbar_A1458) was produced in E. coli and purified indicating that this protein most likely contains two [4Fe-4S] clusters. Using an in vitro enzyme activity assay it was demonstrated that AhbD catalyzes the conversion of iron-coproporphyrin III into heme.
doi_str_mv 10.1155/2014/327637
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In contrast to eukaryotes and most bacteria which employ the so-called “classical” heme biosynthesis pathway, the archaea use an alternative route. In this pathway, heme is formed from uroporphyrinogen III via the intermediates precorrin-2, sirohydrochlorin, siroheme, 12,18-didecarboxysiroheme, and iron-coproporphyrin III. In this study the heme biosynthesis proteins AhbAB, AhbC, and AhbD from Methanosarcina barkeri were functionally characterized. Using an in vivo enzyme activity assay it was shown that AhbA and AhbB (Mbar_A1459 and Mbar_A1460) together catalyze the conversion of siroheme into 12,18-didecarboxysiroheme. The two proteins form a heterodimeric complex which might be subject to feedback regulation by the pathway end-product heme. Further, AhbC (Mbar_A1793) was shown to catalyze the formation of iron-coproporphyrin III in vivo. 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Using an in vitro enzyme activity assay it was demonstrated that AhbD catalyzes the conversion of iron-coproporphyrin III into heme.</description><identifier>ISSN: 1472-3646</identifier><identifier>EISSN: 1472-3654</identifier><identifier>DOI: 10.1155/2014/327637</identifier><identifier>PMID: 24669201</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Limiteds</publisher><subject>Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Bacteria ; Biosynthesis ; Biosynthetic Pathways - genetics ; Enzymes ; Genetic aspects ; Genomes ; Heme ; Heme - biosynthesis ; Methanobacteriaceae ; Methanosarcina barkeri - enzymology ; Methanosarcina barkeri - genetics ; Methanosarcina barkeri - metabolism ; Microbiological synthesis ; Properties ; Protein Multimerization ; Proteins ; Retention ; Uroporphyrinogens - metabolism</subject><ispartof>Archaea, 2014-01, Vol.2014 (2014), p.58-70</ispartof><rights>Copyright © 2014 Melanie Kühner et al.</rights><rights>COPYRIGHT 2014 John Wiley &amp; Sons, Inc.</rights><rights>Copyright © 2014 Melanie Kühner et al. Melanie Kühner et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2014 Melanie Kühner et al. 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a563t-5d3c7d31e081fd0574624db31f88c1cd59d84e16aff2b3d5653f3a6ed62df983</citedby><cites>FETCH-LOGICAL-a563t-5d3c7d31e081fd0574624db31f88c1cd59d84e16aff2b3d5653f3a6ed62df983</cites><orcidid>0000-0001-5927-1671 ; 0000-0002-1569-3431</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1503652326/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1503652326?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,36990,44566,53766,53768,74869</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24669201$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Whitman, William B.</contributor><creatorcontrib>Kühner, Melanie</creatorcontrib><creatorcontrib>Haufschildt, Kristin</creatorcontrib><creatorcontrib>Neumann, Alexander</creatorcontrib><creatorcontrib>Storbeck, Sonja</creatorcontrib><creatorcontrib>Streif, Judith</creatorcontrib><creatorcontrib>Layer, Gunhild</creatorcontrib><title>The Alternative Route to Heme in the Methanogenic Archaeon Methanosarcina barkeri</title><title>Archaea</title><addtitle>Archaea</addtitle><description>In living organisms heme is formed from the common precursor uroporphyrinogen III by either one of two substantially different pathways. 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subjects Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Bacteria
Biosynthesis
Biosynthetic Pathways - genetics
Enzymes
Genetic aspects
Genomes
Heme
Heme - biosynthesis
Methanobacteriaceae
Methanosarcina barkeri - enzymology
Methanosarcina barkeri - genetics
Methanosarcina barkeri - metabolism
Microbiological synthesis
Properties
Protein Multimerization
Proteins
Retention
Uroporphyrinogens - metabolism
title The Alternative Route to Heme in the Methanogenic Archaeon Methanosarcina barkeri
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