- Photosynthetic Processes and Mechanisms
- ATP Synthase and ATPases Research
- Coenzyme Q10 studies and effects
- Bacterial Genetics and Biotechnology
- Mitochondrial Function and Pathology
- Essential Oils and Antimicrobial Activity
- X-ray Diffraction in Crystallography
- Neonatal Health and Biochemistry
- Crystallization and Solubility Studies
- Hemoglobin structure and function
- Bioactive Compounds and Antitumor Agents
- Protein Structure and Dynamics
- Mass Spectrometry Techniques and Applications
- Lipid Membrane Structure and Behavior
Max Planck Institute of Biophysics
2019-2022
Hemes switch spots in a terminal oxidase Reduction of molecular oxygen to water is the driving force for respiration aerobic organisms and catalyzed by several distinct integral membrane complexes. These include an exclusively prokaryotic enzyme, cytochrome bd–type quinol oxidase, which potential antimicrobial target. Safarian et al. determined high-resolution cryo–electron microscopy structure this enzyme from enteric bacterium Escherichia coli . Comparison homolog reveals complete...
New drugs are urgently needed to combat the global TB epidemic. Targeting simultaneously multiple respiratory enzyme complexes of Mycobacterium tuberculosis is regarded as one most effective treatment options shorten drug administration regimes, and reduce opportunity for emergence resistance. During infection proliferation, cytochrome bd oxidase plays a crucial role mycobacterial pathophysiology by maintaining aerobic respiration at limited oxygen concentrations. Here, we present cryo-EM...
The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge the 21st century. membrane-embedded respiratory cytochrome bd-type oxygen reductase critical survival factor utilized pathogenic bacteria during infection, proliferation and transition from acute to chronic states. Escherichia coli encodes for two bd isoforms that are both involved in respiration under limited conditions. Mechanistic structural differences between cydABX (Ecbd-I) appCBX...
Abstract Cytochrome bd -type oxidases play a crucial role for survival of pathogenic bacteria during infection and proliferation. This the fact that there are no homologues in mitochondrial respiratory chain qualify cytochrome as potential antimicrobial target. However, few oxidase selective inhibitors have been described so far. In this report, inhibitory effects Aurachin C (AurC-type) new D (AurD-type) derivatives on oxygen reductase activity isolated terminal -I, -II bo 3 from Escherichia...
Nicotinamide nucleotide transhydrogenases are integral membrane proteins that utilizes the proton motive force to reduce NADP+ NADPH while converting NADH NAD+. Atomic structures of various in different ligand-bound states have become available, and it is clear molecular mechanism involves major conformational changes. Here we utilized hydrogen-deuterium-exchange mass spectrometry (HDX-MS) map ligand binding sites analyzed structural dynamics E. coli transhydrogenase. We found allosteric...
The respiratory chain of Escherichia coli contains two different types terminal oxidase that are differentially regulated as a response to changing environmental conditions. These oxidoreductases catalyze the reduction molecular oxygen water and contribute proton motive force. cytochrome bo