Gottfried Unden

ORCID: 0000-0003-4906-1835
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Research Areas
  • Bacterial Genetics and Biotechnology
  • Amino Acid Enzymes and Metabolism
  • Enzyme Structure and Function
  • RNA and protein synthesis mechanisms
  • Microbial Fuel Cells and Bioremediation
  • Microbial Metabolic Engineering and Bioproduction
  • Photosynthetic Processes and Mechanisms
  • Metalloenzymes and iron-sulfur proteins
  • Bacteriophages and microbial interactions
  • Antibiotic Resistance in Bacteria
  • Protein Structure and Dynamics
  • Hemoglobin structure and function
  • Probiotics and Fermented Foods
  • Metabolism and Genetic Disorders
  • Drug Transport and Resistance Mechanisms
  • Metal-Catalyzed Oxygenation Mechanisms
  • ATP Synthase and ATPases Research
  • Polyamine Metabolism and Applications
  • Mitochondrial Function and Pathology
  • Lipid Membrane Structure and Behavior
  • Fermentation and Sensory Analysis
  • Vitamin K Research Studies
  • Wastewater Treatment and Nitrogen Removal
  • Legume Nitrogen Fixing Symbiosis
  • Electrochemical sensors and biosensors

Johannes Gutenberg University Mainz
2016-2025

University of Applied Sciences Mainz
1995-2023

Institute for Molecular Medicine
2022

Princeton University
2015

Ewha Womans University
2010

Goethe University Frankfurt
1987-2006

Max Planck Institute of Biophysics
2006

Heinrich Heine University Düsseldorf
1991-1995

Philipps University of Marburg
1981-1986

University of Sheffield
1984

Summary The function of the LysR‐type regulator LrhA Escherichia coli was defined by comparing whole‐genome mRNA profiles from wild‐type E. and an isogenic lrhA mutant on a DNA microarray. In mutant, large number (48) genes involved in flagellation, motility chemotaxis showed relative abundances increased factors between 3 80. When representative set five flagellar, tested lacZ reporter gene fusions, similar for derepression were found mutant. gel retardation experiments, protein bound...

10.1046/j.1365-2958.2002.03032.x article EN Molecular Microbiology 2002-07-01

The energetic parameters of Escherichia coli were analyzed for the aerobic/anaerobic transition. electrochemical proton potential (Δ p ) across cytoplasmic membrane was determined in steady state respiration with O 2 , nitrate, fumarate, dimethylsulfoxide (Me SO), and fermentation. With a −160 mV obtained. For anaerobic fumarate or Me SO, Δ decreased only slightly by about 20 contrast to earlier assumptions, whereas dropped approximately 40 during Under all conditions, @KY) contributed major...

10.1046/j.1432-1327.1998.2510538.x article EN European Journal of Biochemistry 1998-01-01

Escherichia coli contains a versatile respiratory chain that oxidizes 10 different electron donor substrates and transfers the electrons to terminal reductases or oxidases for reduction of six acceptors. Salmonella is able use two more The variation further increased by presence isoenzymes some substrates. A large number pathways can be established combining donors dehydrogenases quinones as acceptors are oxidized reductase oxidases. enzymes vary largely with respect their composition,...

10.1128/ecosalplus.esp-0005-2013 article EN EcoSal Plus 2014-10-27

C4-dicarboxylates and the C4-dicarboxylic amino acid l-aspartate support aerobic anaerobic growth of Escherichia coli related bacteria. In growth, succinate, fumarate, D- L-malate, L-aspartate, L-tartrate are metabolized by citric cycle associated reactions. Because interruption under conditions, metabolism depends on fumarate reduction to succinate (fumarate respiration). some bacteria (e.g., Klebsiella), utilization C4-dicarboxylates, such as tartrate, is independent respiration uses a...

10.1128/ecosalplus.esp-0021-2015 article EN EcoSal Plus 2016-11-05

Thiosulfate respiration in Salmonella enterica serovar Typhimurium is catalyzed by the membrane-bound enzyme thiosulfate reductase. Experiments with quinone biosynthesis mutants show that menaquinol sole electron donor to However, reduction of highly endergonic under standard conditions (ΔE°' = -328 mV). reductase activity was found depend on proton motive force (PMF) across cytoplasmic membrane. A structural model for suggests PMF drives flow within a reverse loop mechanism. able catalyze...

10.1128/jb.06014-11 article EN Journal of Bacteriology 2011-11-12

In Escherichia coli the expression of nuo genes encoding proton pumping NADH dehydrogenase I is stimulated by presence fumarate during anaerobic respiration. The regulatory sites required for induction fumarate, nitrate and O 2 are located at positions around –309, –277, downstream –231 bp, respectively, relative to transcriptional‐start site. regulator has be different from O2 regulators ArcA NarL. For growth respiration, was essential, in contrast aerobic or respiration which used...

10.1111/j.1432-1033.1997.00155.x article EN European Journal of Biochemistry 1997-02-01

Succinate dehydrogenases from bacteria and archaea using menaquinone (MK) as an electron acceptor (succinate/menaquinone oxidoreductases) contain, or are predicted to two heme‐B groups in the membrane‐anchoring protein(s), located close opposite sides of membrane. All succinate/ubiquinone oxidoreductases, however, contain only one molecule. In Bacillus subtilis other that use MK respiratory quinone, succinate oxidase activity (succinate←O 2 ), succinate/menaquinone oxidoreductase were...

10.1046/j.1432-1327.1998.2570210.x article EN European Journal of Biochemistry 1998-10-01

ABSTRACT In Escherichia coli the genes encoding anaerobic fumarate respiratory system are transcriptionally regulated by C 4 -dicarboxylates. The regulation is effected a two-component regulatory system, DcuSR, consisting of sensory histidine kinase (DcuS) and response regulator (DcuR). DcuS DcuR encoded dcuSR (previously yjdHG ) at 93.7 min on calculated E. map. Inactivation dcuR dcuS caused loss -dicarboxylate-stimulated synthesis reductase ( frdABCD genes) fumarate-succinate antiporter...

10.1128/jb.180.20.5421-5425.1998 article EN Journal of Bacteriology 1998-10-15

Type 1 fimbriae of Escherichia coli facilitate attachment to the host mucosa and promote biofilm formation on abiotic surfaces. The transcriptional regulator LrhA, which is known as a repressor flagellar, motility chemotaxis genes, regulates expression type fimbriae. Whole-genome profiling revealed that inactivation lrhA results in an increased structural components In vitro , LrhA bound promoter regions two fim recombinases (FimB FimE) catalyse inversion fimA promoter, invertible element...

10.1099/mic.0.28098-0 article EN Microbiology 2005-10-01

With an oxystat, changes in the pattern of expression FNR-dependent genes from Escherichia coli were studied as a function O2 tension (pO2) medium. Expression all four tested was decreased by increasing O2. However, pO2 values that gave rise to half-maximal repression (pO(0.5)) dependent on particular promoter and varied between 1 5 millibars (1 bar = 10(5) Pa). The pO(0.5) value for ArcA-regulated succinate dehydrogenase same range (pO(0.5) 4.6 millibars). At these values, cytoplasm can be...

10.1128/jb.178.15.4515-4521.1996 article EN Journal of Bacteriology 1996-08-01

The nucleotide sequences of two Escherichia coli genes, dcuA and dcuB (formerly designated genA genF), have been shown to encode highly homologous products, M(r) 45,751 47,935 (434 446 amino acid residues) with 36% sequence identity (63% similarity). These proteins a high proportion (approximately 61%) hydrophobic residues are probably members new group integral inner membrane proteins. locations the dcu one upstream aspartase gene (dcuA-aspA) other downstream anaerobic fumarase (fumB-dcuB),...

10.1128/jb.176.21.6470-6478.1994 article EN Journal of Bacteriology 1994-11-01

Summary FNR, the transcriptional regulator of gene expression anaerobic respiration in Escherichia coli , contains a cluster cysteine residues at amino terminus which resembles metal‐binding domains proteins. It is possible, therefore, (i) that FNR binds metals with cysteines as ligands and (ii) this property related to regulatory function FNR. These questions were investigated, following results. Approximately 2.4 4 can be alkylated iodoacetate permeabilized aerobic or bacteria without...

10.1111/j.1365-2958.1989.tb00206.x article EN Molecular Microbiology 1989-05-01

The structure of the water-soluble, periplasmic domain fumarate sensor DcuS (DcuS-pd) has been determined by NMR spectroscopy in solution. is a prototype for sensory histidine kinase with transmembrane signal transfer. belongs to CitA family sensors that are specific sensing di- and tricarboxylates. folded autonomously shows helices at N C terminus, suggesting direct linking or connection two regions. constitutes novel fold. nearest structural neighbor Per-Arnt-Sim photoactive yellow protein...

10.1074/jbc.c300344200 article EN cc-by Journal of Biological Chemistry 2003-09-26
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