Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway

Authors: Paolo Olivieri, Moritz Klabes, Jason C. Crack, Angelika Lehmann, Sophie P. Bennett, Nick E. Le Brun, Silke Leimkühler

Source: Microbiology Spectrum, Vol 12, Iss 8 (2024)

Subject Terms: IscS, Fe-S cluster, iron, sulfur, cysteine desulfurase, Microbiology, QR1-502

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Relation: https://doaj.org/toc/2165-0497

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TusA influences Fe-S cluster assembly and iron homeostasis in E. coli by reducing the translation efficiency of Fur

Authors: Paolo Olivieri, Arkadiuz Zupok, Tugba Yildiz, Jonathan Oltmanns, Angelika Lehmann, Ewelina Sokolowska, Aleksandra Skirycz, Volker Schünemann, Silke Leimkühler

Source: Microbiology Spectrum, Vol 12, Iss 8 (2024)

Subject Terms: iron uptake, sulfur, iron metabolism, Fe-S, tRNA modification, translation, Microbiology, QR1-502

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Relation: https://doaj.org/toc/2165-0497

Access URL: https://doaj.org/article/1c0f1b057c07423385460977d3c5e140

Biocatalytic cofactor regeneration for CO2 reduction: Integration of a hydrogenase and a formate dehydrogenase in H2-driven systems

Authors: Michael Groh, Elisabeth Lettau, Janna Schoknecht, Jan Liedtke, Lars Lauterbach, Silke Leimkühler

Source: Journal of CO2 Utilization, Vol 83, Iss , Pp 102828- (2024)

Subject Terms: Formate, Carbon dioxide, Molybdenum, Iron-sulfur, Cascade reaction, Technology

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S221298202400163X; https://doaj.org/toc/2212-9839

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Iron limitation indirectly reduces the Escherichia coli torCAD operon expression by a reduction of molybdenum cofactor availability

Authors: Muhammad Abrar Hasnat, Arkadiusz Zupok, Michal Gorka, Chantal Iobbi-Nivol, Aleksandra Skirycz, Cécile Jourlin-Castelli, Frank Bier, Saloni Agarwal, Ehizode Irefo, Silke Leimkühler

Source: Microbiology Spectrum, Vol 12, Iss 2 (2024)

Subject Terms: iron regulation, Escherichia coli, molybdenum cofactor, FNR, iron-sulfur cluster, anaerobic respiration, Microbiology, QR1-502

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Relation: https://doaj.org/toc/2165-0497

Access URL: https://doaj.org/article/1aa3febca90743e79ae94752245b5131

E. coli MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase

Authors: Moses Ogunkola, Lennart Wolff, Eric Asare Fenteng, Benjamin R. Duffus, Silke Leimkühler

Source: Inorganics, Vol 12, Iss 3, p 67 (2024)

Subject Terms: tRNA, thiouridine, iron–sulfur cluster, Inorganic chemistry, QD146-197

File Description: electronic resource

Relation: https://www.mdpi.com/2304-6740/12/3/67; https://doaj.org/toc/2304-6740

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Metal-Containing Formate Dehydrogenases, a Personal View

Authors: Silke Leimkühler

Source: Molecules, Vol 28, Iss 14, p 5338 (2023)

Subject Terms: molybdoenzymes, bis-MGD, formate oxidation, CO2 reduction, oxygen atom transfer, Organic chemistry, QD241-441

File Description: electronic resource

Relation: https://www.mdpi.com/1420-3049/28/14/5338; https://doaj.org/toc/1420-3049

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The Mechanism of Metal-Containing Formate Dehydrogenases Revisited: The Formation of Bicarbonate as Product Intermediate Provides Evidence for an Oxygen Atom Transfer Mechanism

Authors: Hemant Kumar, Maryam Khosraneh, Siva S. M. Bandaru, Carola Schulzke, Silke Leimkühler

Source: Molecules, Vol 28, Iss 4, p 1537 (2023)

Subject Terms: molybdoenzyme, formate dehydrogenase, oxygen atom transfer, Rhodobactor capsulatus, Organic chemistry, QD241-441

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Relation: https://www.mdpi.com/1420-3049/28/4/1537; https://doaj.org/toc/1420-3049

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Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase

Authors: Christin Radon, Gerd Mittelstädt, Benjamin R. Duffus, Jörg Bürger, Tobias Hartmann, Thorsten Mielke, Christian Teutloff, Silke Leimkühler, Petra Wendler

Source: Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)

Subject Terms: Science

File Description: electronic resource

Relation: https://doaj.org/toc/2041-1723

Access URL: https://doaj.org/article/ee6fb5dae1e445018b0579d644893722

The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells

Authors: Moses Olalekan Ogunkola, Gaelle Guiraudie-Capraz, Francois Feron, Silke Leimkühler

Source: Biomolecules, Vol 13, Iss 1, p 144 (2023)

Subject Terms: Moco biosynthesis, sulfite oxidase, cytosolic tRNA thiolation, 5-methoxycarbonylmethyl-2-thiouridine, H2S biosynthesis, cellular bioenergetics, Microbiology, QR1-502

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Relation: https://www.mdpi.com/2218-273X/13/1/144; https://doaj.org/toc/2218-273X

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Human aldehyde oxidase (hAOX1): structure determination of the Moco‐free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms

Authors: Cristiano Mota, Mariam Esmaeeli, Catarina Coelho, Teresa Santos‐Silva, Martin Wolff, Alessandro Foti, Silke Leimkühler, Maria João Romão

Source: FEBS Open Bio, Vol 9, Iss 5, Pp 925-934 (2019)

Subject Terms: human aldehyde oxidase, molybdenum cofactor, single nucleotide polymorphism, xanthine oxidase, Biology (General), QH301-705.5

File Description: electronic resource

Relation: https://doaj.org/toc/2211-5463

Access URL: https://doaj.org/article/a305ef19af68434e80950374136dd979

The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes

Authors: Kim Tiedemann, Chantal Iobbi-Nivol, Silke Leimkühler

Source: Molecules, Vol 27, Iss 9, p 2993 (2022)

Subject Terms: bis-MGD, chaperone, molybdenum cofactor, TMAO reductase, Organic chemistry, QD241-441

File Description: electronic resource

Relation: https://www.mdpi.com/1420-3049/27/9/2993; https://doaj.org/toc/1420-3049

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The sulfite oxidase Shopper controls neuronal activity by regulating glutamate homeostasis in Drosophila ensheathing glia

Authors: Nils Otto, Zvonimir Marelja, Andreas Schoofs, Holger Kranenburg, Jonas Bittern, Kerem Yildirim, Dimitri Berh, Maria Bethke, Silke Thomas, Sandra Rode, Benjamin Risse, Xiaoyi Jiang, Michael Pankratz, Silke Leimkühler, Christian Klämbt

Source: Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)

Subject Terms: Science

File Description: electronic resource

Relation: https://doaj.org/toc/2041-1723

Access URL: https://doaj.org/article/1d164f61f1ee44d3bf7f3ff6c54fc0ab

ecoAO: A Simple System for the Study of Human Aldehyde Oxidases Role in Drug Metabolism

Authors: Erickson M. Paragas, Sara C. Humphreys, Joshua Min, Carolyn A. Joswig-Jones, Silke Leimkühler, Jeffrey P. Jones

Source: ACS Omega, Vol 2, Iss 8, Pp 4820-4827 (2017)

Subject Terms: Chemistry, QD1-999

File Description: electronic resource

Relation: https://doaj.org/toc/2470-1343

Access URL: https://doaj.org/article/542e50e901754d959494d5128a837e11

Electrochemical Trimethylamine N-Oxide Biosensor with Enzyme-Based Oxygen-Scavenging Membrane for Long-Term Operation under Ambient Air

Authors: Armel F. T. Waffo, Biljana Mitrova, Kim Tiedemann, Chantal Iobbi-Nivol, Silke Leimkühler, Ulla Wollenberger

Source: Biosensors, Vol 11, Iss 4, p 98 (2021)

Subject Terms: trimethylamine N-oxide, biosensor, TMAO-reductase, oxygen scavenger, immobilized enzyme, multienzyme electrode, Biotechnology, TP248.13-248.65

File Description: electronic resource

Relation: https://www.mdpi.com/2079-6374/11/4/98; https://doaj.org/toc/2079-6374

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Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems

Authors: Silke Leimkühler

Source: Inorganics, Vol 9, Iss 1, p 6 (2021)

Subject Terms: n/a, Inorganic chemistry, QD146-197

File Description: electronic resource

Relation: https://www.mdpi.com/2304-6740/9/1/6; https://doaj.org/toc/2304-6740

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The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

Authors: Ralf R. Mendel, Thomas W. Hercher, Arkadiusz Zupok, Muhammad A. Hasnat, Silke Leimkühler

Source: Inorganics, Vol 8, Iss 7, p 43 (2020)

Subject Terms: Moco biosynthesis, Fe-S cluster assembly, l-cysteine desulfurase, ISC, SUF, NIF, Inorganic chemistry, QD146-197

File Description: electronic resource

Relation: https://www.mdpi.com/2304-6740/8/7/43; https://doaj.org/toc/2304-6740

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The ABCB7-Like Transporter PexA in Rhodobacter capsulatus Is Involved in the Translocation of Reactive Sulfur Species

Authors: Simona Riedel, Beata Siemiatkowska, Mutsumi Watanabe, Christina S. Müller, Volker Schünemann, Rainer Hoefgen, Silke Leimkühler

Source: Frontiers in Microbiology, Vol 10 (2019)

Subject Terms: ABCB7, persulfide, polysulfide, glutathione, ABC transporter, Walker A motif, Microbiology, QR1-502

File Description: electronic resource

Relation: https://www.frontiersin.org/article/10.3389/fmicb.2019.00406/full; https://doaj.org/toc/1664-302X

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Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

Authors: Zvonimir Marelja, Silke Leimkühler, Fanis Missirlis

Source: Frontiers in Physiology, Vol 9 (2018)

Subject Terms: aldehyde oxidase, DNA polymerase, electron transport chain, ecdysone, iron regulatory protein, quiescent mitochondria, Physiology, QP1-981

File Description: electronic resource

Relation: http://journal.frontiersin.org/article/10.3389/fphys.2018.00050/full; https://doaj.org/toc/1664-042X

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Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.

Authors: Nadine Schwanhold, Chantal Iobbi-Nivol, Angelika Lehmann, Silke Leimkühler

Source: PLoS ONE, Vol 13, Iss 11, p e0201935 (2018)

Subject Terms: Medicine, Science

File Description: electronic resource

Relation: http://europepmc.org/articles/PMC6239281?pdf=render; https://doaj.org/toc/1932-6203

Access URL: https://doaj.org/article/4df89998ab534843943060eb0d01c4e5

Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities.

Authors: Gökhan Kücükgöze, Silke Leimkühler

Source: PLoS ONE, Vol 13, Iss 1, p e0191819 (2018)

Subject Terms: Medicine, Science

File Description: electronic resource

Relation: http://europepmc.org/articles/PMC5784979?pdf=render; https://doaj.org/toc/1932-6203

Access URL: https://doaj.org/article/4e6eacd9b25447d3a92e59629462a42f