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  1. Article ; Online: Heme biosynthesis in prokaryotes.

    Layer, Gunhild

    Biochimica et biophysica acta. Molecular cell research

    2020  Volume 1868, Issue 1, Page(s) 118861

    Abstract: The cyclic tetrapyrrole heme is used as a prosthetic group in a broad variety of different proteins in almost all organisms. Often, it is essential for vital biochemical processes such as aerobic and anaerobic respiration as well as photosynthesis. In ... ...

    Abstract The cyclic tetrapyrrole heme is used as a prosthetic group in a broad variety of different proteins in almost all organisms. Often, it is essential for vital biochemical processes such as aerobic and anaerobic respiration as well as photosynthesis. In Nature, heme is made from the common tetrapyrrole precursor 5-aminolevulinic acid, and for a long time it was assumed that heme is biosynthesized by a single, common pathway in all organisms. However, although this is indeed the case in eukaryotes, heme biosynthesis is more diverse in the prokaryotic world, where two additional pathways exist. The final elucidation of the two 'alternative' heme biosynthesis routes operating in some bacteria and archaea was achieved within the last decade. This review summarizes the three different heme biosynthesis pathways with a special emphasis on the two 'new' prokaryotic routes.
    MeSH term(s) Aerobiosis/genetics ; Aminolevulinic Acid/metabolism ; Anaerobiosis/genetics ; Archaea/genetics ; Bacteria/genetics ; Heme/biosynthesis ; Heme/genetics ; Photosynthesis/genetics ; Prokaryotic Cells/metabolism ; Tetrapyrroles/genetics ; Tetrapyrroles/metabolism
    Chemical Substances Tetrapyrroles ; Heme (42VZT0U6YR) ; Aminolevulinic Acid (88755TAZ87)
    Language English
    Publishing date 2020-09-23
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2020.118861
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Radical SAM Enzymes Involved in Tetrapyrrole Biosynthesis and Insertion.

    Layer, Gunhild / Jahn, Martina / Moser, Jürgen / Jahn, Dieter

    ACS bio & med chem Au

    2022  Volume 2, Issue 3, Page(s) 196–204

    Abstract: The anaerobic biosyntheses of heme, ... ...

    Abstract The anaerobic biosyntheses of heme, heme
    Language English
    Publishing date 2022-02-16
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2694-2437
    ISSN (online) 2694-2437
    DOI 10.1021/acsbiomedchemau.1c00061
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The Radical SAM Heme Synthase AhbD from

    Fix, Isabelle / Heidinger, Lorenz / Friedrich, Thorsten / Layer, Gunhild

    Biomolecules

    2023  Volume 13, Issue 8

    Abstract: In archaea and sulfate-reducing bacteria, heme is synthesized via the siroheme-dependent pathway. The last step of this route is catalyzed by the Radical SAM enzyme AhbD and consists of the conversion of iron-coproporphyrin III into heme. AhbD belongs to ...

    Abstract In archaea and sulfate-reducing bacteria, heme is synthesized via the siroheme-dependent pathway. The last step of this route is catalyzed by the Radical SAM enzyme AhbD and consists of the conversion of iron-coproporphyrin III into heme. AhbD belongs to the subfamily of Radical SAM enzymes containing a SPASM/Twitch domain carrying either one or two auxiliary iron-sulfur clusters in addition to the characteristic Radical SAM cluster. In previous studies, AhbD was reported to contain one auxiliary [4Fe-4S] cluster. In this study, the amino acid sequence motifs containing conserved cysteine residues in AhbD proteins from different archaea and sulfate-reducing bacteria were reanalyzed. Amino acid sequence alignments and computational structural models of AhbD suggested that a subset of AhbD proteins possesses the full SPASM motif and might contain two auxiliary iron-sulfur clusters (AuxI and AuxII). Therefore, the cluster content of AhbD from
    MeSH term(s) Methanosarcina barkeri ; Ferrochelatase ; Archaea ; Heme ; Iron ; Sulfates
    Chemical Substances Ferrochelatase (EC 4.99.1.1) ; Heme (42VZT0U6YR) ; Iron (E1UOL152H7) ; Sulfates
    Language English
    Publishing date 2023-08-18
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom13081268
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Book ; Online ; Thesis: <dc:title>Charakterisierung der Eisen-Schwefel-Cluster der Häm-Synthase AhbD aus Methanosarcina barkeri</dc:title>

    Fix, Isabelle [Verfasser] / Layer, Gunhild [Akademischer Betreuer] / Layer, Gunhild / Friedrich, Thorsten

    2022  

    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language German
    Publisher Universität
    Publishing place Freiburg
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  5. Article ; Online: Characterization of the iron-sulfur clusters in the nitrogenase-like reductase CfbC/D required for coenzyme F

    Vazquez Ramos, José / Kulka-Peschke, Catharina J / Bechtel, Dominique F / Zebger, Ingo / Pierik, Antonio J / Layer, Gunhild

    The FEBS journal

    2024  

    Abstract: ... Coenzyme ... ...

    Abstract Coenzyme F
    Language English
    Publishing date 2024-04-08
    Publishing country England
    Document type Journal Article
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.17134
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Book ; Online ; Thesis: anaerobic cyclase BchE from Rhodobacter capsulatus is a cobalamin-dependent radical SAM enzyme

    Wiesselmann, Milan Jonas Verfasser] / [Jahn, Dieter [Akademischer Betreuer] / Layer, Gunhild [Akademischer Betreuer]

    2023  

    Author's details Milan Jonas Wiesselmann ; Dieter Jahn, Gunhild Layer
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Technische Universität Braunschweig
    Publishing place Braunschweig
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  7. Book ; Thesis: Biosynthesis of iron-sulfur clusters and tetrapyrroles in microorganisms

    Layer, Gunhild

    2015  

    Author's details von Gunhild Layer
    Language English
    Size Getr. Zählung [226 S.], Ill., graph. Darst.
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Techn. Univ., kumulative Habil.-Schr.--Braunschweig, 2012
    Note Zsfassung in engl. Sprache ; Enth. 10 Zeitschr.aufsätze
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  8. Book ; Online ; Thesis: <dc:title>Biochemische Untersuchungen zu NirN und NirF aus Pseudomonas aeruginosa</dc:title>

    Preuß, Arne [Verfasser] / Layer, Gunhild [Akademischer Betreuer]

    2021  

    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language German
    Publisher Universität
    Publishing place Freiburg
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  9. Article ; Online: Enzymatic Systems with Homology to Nitrogenase: Biosynthesis of Bacteriochlorophyll and Coenzyme F

    Moser, Jürgen / Layer, Gunhild

    Methods in molecular biology (Clifton, N.J.)

    2018  Volume 1876, Page(s) 25–35

    Abstract: Enzymes with homology to nitrogenase are essential for the reduction of chemically stable double bonds within the biosynthetic pathways of bacteriochlorophyll and coenzyme ... ...

    Abstract Enzymes with homology to nitrogenase are essential for the reduction of chemically stable double bonds within the biosynthetic pathways of bacteriochlorophyll and coenzyme F
    MeSH term(s) Adenosine Triphosphate/metabolism ; Alcohol Oxidoreductases/chemistry ; Alcohol Oxidoreductases/metabolism ; Archaea/chemistry ; Archaea/enzymology ; Archaeal Proteins/chemistry ; Archaeal Proteins/metabolism ; Bacteriochlorophylls/biosynthesis ; Catalysis ; Metalloporphyrins/metabolism ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/metabolism ; Nickel ; Nitrogenase/chemistry ; Sequence Homology, Amino Acid
    Chemical Substances Archaeal Proteins ; Bacteriochlorophylls ; Metalloporphyrins ; Multienzyme Complexes ; factor F430 (73145-13-8) ; Nickel (7OV03QG267) ; Adenosine Triphosphate (8L70Q75FXE) ; Alcohol Oxidoreductases (EC 1.1.-) ; Nitrogenase (EC 1.18.6.1)
    Language English
    Publishing date 2018-10-13
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-8864-8_2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Book ; Online ; Thesis: Nitrogenase-like Biosynthesis of (Bacterio)chlorophylls

    Jasper, Jan Verfasser] / [Jahn, Dieter [Akademischer Betreuer] / Layer, Gunhild [Akademischer Betreuer]

    2021  

    Author's details Jan Jasper ; Dieter Jahn, Gunhild Layer
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Technische Universität Braunschweig
    Publishing place Braunschweig
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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