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Publikationen

der Arbeitsgruppe von Prof. Dr. Gunhild Layer

 

2023 2022  2021  2020  2019  2018  2017  2016  2014  2013  2012  2011  2010  2009  vor 2009

 

2023

Fix I., Heidinger L., Friedrich T. & Layer G. (2023) The Radical SAM heme synthase AhbD from Methanosarcina barkeri contains two auxiliary [4Fe-4S] clusters.

Biomolecules, 13, 1268.

Gericke L., Mhaindarkar D., Karst L.C., Jahn S., Kuge M., Mohr M.K.F., Gagsteiger J., Cornelissen N.V., Wen X., Mordhorst S., Jessen H.J., Rentmeister A., Seebeck F.P., Layer G., Loenarz C. & Andexer J.N. (2023) Biomimetic S-adenosylmethionine regeneration starting from multiple byproducts enables biocatalytic alkylation with Radical SAM enzymes.

Chembiochem., 24, e202300133.

2022

Gagsteiger J., Jahn, S., Heidinger L., Gericke L., Andexer J.N., Friedrich T., Lönarz C. & Layer G. (2022) A cobalamin-dependent Radical SAM enzyme catalyzes the unique Cα-methylation of glutamine in methyl-coenzyme M reductase.

Angew. Chem. Int. Ed., 61, e202204198.

Layer G., Jahn M., Moser J. & Jahn D. (2022) Radical SAM enzymes involved in tetrapyrrole biosynthesis and insertion.

ACS Bio. Med. Chem. Au, 2, 196-204.

2021

Layer G. (2021) Heme biosynthesis in prokaryotes.

BBA - Molecular Cell Research, 1868, 118861.

Klünemann T., Nimtz M., Jänsch L., Layer G. & Blankenfeldt W. (2021) Crystal structure of NirF: insights into its role in heme d1 biosynthesis.

FEBS J., 288, 244-261.

2020

Layer G. (2020) Radical S-adenosylmethionine enzymes in heme biosynthesis.

In: Hung-Wen (Ben) Liu and Tadhg P. Begley (eds.), Comprehensive Natural Products III: Chemistry and Biology, Volume 5, 349-363.

Jasper J., Vazquez Ramos J., Trncik C., Jahn D., Einsle O., Layer G. & Moser J. (2020) Chimeric interaction of nitrogenase-like reductases with the MoFe protein of nitrogenase.

Chembiochem, 21, 1733-1741.

Deobald D., Hanna R., Shahryari S., Layer G. & Adrian L. (2020) Identification and characterization of a bacterial core methionine synthase.

Sci. Rep., 10, 2100.

2019

Fan T., Grimm B. & Layer G. (2019) Porphyrin and heme synthesis.

in "Advances in Botanical Research", 91, 89-131.

Klünemann T., Preuß A., Adamczack J., Rosa L.F.M., Harnisch F., Layer G. & Blankenfeldt W. (2019) Crystal structure of dihydro-heme d1 dehydrogenase NirN from Pseudomonas aeruginosa reveals amino acid residues essential for catalysis.

J. Mol. Biol., 431, 3246-3260.

Moser J. & Layer G. (2019) Enzymatic systems with homology to nitrogenase: Biosynthesis of bacteriochlorophyll and coenzyme F430.

Methods Mol. Biol., 1876, 25-35.

Moser J., Jasper J., Vazquez Ramos J., Sowa S.T. & Layer G. (2019) Expression, purification, and activity analysis of chlorophyllide oxidoreductase and Ni2+-sirohydrochlorin a,c-diamide reductase.

Methods Mol. Biol., 1876, 125-140.

2018

Deobald D., Adrian L., Schöne C., Rother M. & Layer G. (2018) Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase.

Sci. Rep., 8, 7404. 

2017

Boss L., Oehme R., Billig S., Birkemeyer C. & Layer G. (2017) The Radical SAM enzyme NirJ catalyzes the removal of two propionate side chains during heme d1 biosynthesis.

FEBS J., 284, 4314-4327.

Moore S.J., Sowa S.T., Schuchardt C., Deery E., Lawrence A.D., Ramos J.V., Billig S., Birkemeyer C., Chivers P.T., Howard M.J., Rigby S.E., Layer G. & Warren M.J. (2017) Elucidation of the biosynthesis of the methane catalyst coenzyme F430.

Nature, 543, 78-82.

Layer G., Krausze J. & Moser J. (2017) Reduction of chemically stable multibonds: Nitrogenase-like biosynthesis of tetrapyrroles.

Adv. Exp. Med. Biol., 925, 147-161.

2016

Layer G. (2016) Siroheme decarboxylase in complex with iron-uroporphyrin III.

in "Encyclopedia of Inorganic and Bioinorganic Chemistry", ed R.A. Scott, John Wiley, Chichester.

Kühner M., Schweyen P., Hoffmann M., Vazquez Ramos J., Reijerse E.J., Lubitz W., Bröring M. & Layer G. (2016) The auxiliary [4Fe-4S] cluster of the Radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer.

Chem. Sci., 7, 4633-43.

2014

Adamczack J., Hoffmann M., Papke U., Haufschildt K., Nicke T., Bröring M., Sezer M., Weimar R., Kuhlmann U., Hildebrandt P. & Layer G. (2014) NirN from Pseudomonas aeruginosa is a novel electron-bifurcating dehydrogenase catalyzing the last step of heme d1 biosynthesis.

J. Biol. Chem., 289, 30753-62.

Haufschildt K., Schmelz S., Kriegler T.M., Neumann A., Streif J., Arai H., Heinz D.W. & Layer G. (2014) The crystal structure of siroheme decarboxylase in complex with iron-uroporphyrin III reveals two essential histidine residues.

J. Mol. Biol., 426, 3272-86.

Kühner M., Haufschildt K., Neumann A., Storbeck S., Streif J. & Layer G. (2014) The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri.

Archaea, 2014, Article ID 327637.

2013

Nicke T., Schnitzer T., Münch K., Adamczack J., Haufschildt K., Buchmeier S., Kucklick M., Riedel K., Felgenträger U., Jänsch L. & Layer G. (2013) Maturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF.

Biosci. Rep., 33, art:e00048.

Kaufholz A.-L., Hunter G. A., Ferreira G. A., Lendrihas T., Hering V., Layer G., Jahn M. & Jahn D. (2013) Aminolevulinic acid synthase of Rhodobacter capsulatus - high resolution kinetic investigation of the structural basis for substrate binding and catalysis.

Biochem. J., 451, 205-16.

2012

Abicht H.K., Martinez J., Layer G., Jahn D. & Solioz M. (2012) Lactococcus lactis HemW (HemN) is a heme-binding protein with a putative role in heme trafficking.

Biochem. J., 442, 335-43.

2011

Layer G. & Warren M.J. (2011) Biosynthesis of siroheme, cofactor F430 and heme d1.

Handbook of Porphyrin Science19, 111-38.

Storbeck S., Saha S., Krausze J., Klink B.U., Heinz D.W. & Layer G. (2011) Crystal structure of the heme d1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-adenosyl-L-methionine dependent uroporphyrinogen III methyltransferases.

J. Biol. Chem., 286, 26754-67.

Layer G., Jahn D. & Jahn M. (2011) Heme biosynthesis.

Handbook of Porphyrin Science15, 159-215.

2010

Storbeck S., Rolfes S., Raux-Deery E., Warren M.J., Jahn D. & Layer G. (2010) A novel pathway for the biosynthesis of heme in Archaea: Genome-based bioinformatic predictions and experimental evidence.

Archaea, 2010, ID 175050.

Wollers S., Layer G., Garcia-Serres R., Signor L., Clemancey M., Latour JM., Fontecave M. & Ollagnier-de Choudens S. (2010) Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor.

J. Biol. Chem., 285, 23331-41.

Layer G., Reichelt J., Jahn D. & Heinz D.W. (2010) Structure and function of enzymes in heme biosynthesis.

Protein Science, 19, 1137-61.

Rand K., Noll C., Schiebel H.M., Kemken D., Dülcks T., Kalesse M., Heinz D.W. & Layer G. (2010)  Oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III into protoporphyrinogen IX.

Biol. Chem., 391, 55-63.

Layer G., Jahn D., Deery E., Lawrence A.D. & Warren M.J. (2010) Biosynthesis of heme and vitamin B12.

in "Comprehensive Natural Products II, Chemistry and Biology" (Mander, L., Lui, H.-W.) Elsevier: Oxford; 7, 445–99.

2009

Storbeck S., Walther J., Müller J., Parmar V., Schiebel H.M., Kemken D., Dülcks T., Warren M.J. & Layer G. (2009) The Pseudomonas aeruginosa nirE gene encodes the S-adenosyl-L-methionine dependent uroporphyrinogen III methyltransferase required for heme d1 biosynthesis.

FEBS J., 276, 5973-82.

vor 2009

Layer G., Gaddam S.A., Ayala-Castro C.N., Ollagnier-de Choudens S., Lascoux D., Fontecave M. & Outten F.W. (2007) SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly.

J. Biol. Chem., 282, 13342-50.

Layer G., Ollagnier-de Choudens S., Sanakis Y. & Fontecave M. (2006) Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CyaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU.

J. Biol. Chem., 281, 16256-63.

Layer G., Pierik A.J., Trost M., Rigby S.E., Leech H.K., Grage K., Breckau D., Astner I., Jänsch L., Heathcote P., Warren M.J., Heinz D.W. & Jahn D. (2006) The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN.

J. Biol. Chem., 281, 15727-34.

Reents H., Gruner I., Harmening U., Böttger L.H., Layer G., Heathcote P., Trautwein A.X., Jahn D. & Härtig E. (2006) Bacillus subtilis Fnr senses oxygen via a [4Fe-4S] cluster coordinated by three cysteine residues without change in the oligomeric state.

Mol. Microbiol., 60, 1432-45.

Layer G., Grage K., Teschner T., Schünemann V., Breckau D., Masoumi A., Jahn M., Heathcote P., Trautwein A.X. & Jahn D. (2005) Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines.

J. Biol. Chem., 280, 29038-46.

Layer G., Kervio E., Morlock G., Heinz D.W., Jahn D., Retey J. & Schubert W.D. (2005) Structural and functional comparison of HemN to other radical SAM enzymes.

Biol. Chem., 386, 971-80.

Layer G., Heinz D.W., Jahn D. & Schubert W.D. (2004) Structure and function of Radical SAM enzymes.

Curr. Opin. Chem. Biol., 8, 468-76.

Layer G., Moser J., Heinz D.W., Jahn D. & Schubert W.D. (2003) Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes.

EMBO J., 22, 6214-24.

Breckau D., Mahlitz E., Sauerwald A., Layer G. & Jahn D. (2003) Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese.

J. Biol. Chem., 278, 46625-31.

Baysse C., Matthijs S., Schobert M., Layer G., Jahn D. & Cornelis P. (2003) Co-ordination of iron acquisition, iron porphyrin chelation and iron-protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens.

Microbiology, 149, 3543-52.

Layer G., Verfürth K., Mahlitz E. & Jahn D. (2002) Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli.

J. Biol. Chem., 277, 34136-42.