Michel A. Struwe

ORCID: 0000-0001-6931-1841
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About
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Research Areas
  • Metalloenzymes and iron-sulfur proteins
  • Drug Transport and Resistance Mechanisms
  • Metal-Organic Frameworks: Synthesis and Applications
  • Liver Disease Diagnosis and Treatment
  • Alcohol Consumption and Health Effects
  • RNA regulation and disease
  • Bacterial Infections and Vaccines
  • Burkholderia infections and melioidosis
  • Sulfur Compounds in Biology
  • Folate and B Vitamins Research
  • Metabolism and Genetic Disorders
  • Bacteriophages and microbial interactions
  • Eicosanoids and Hypertension Pharmacology
  • Electrochemical Analysis and Applications
  • Trace Elements in Health
  • RNA and protein synthesis mechanisms
  • Electron Spin Resonance Studies
  • Pharmacogenetics and Drug Metabolism
  • Metal-Catalyzed Oxygenation Mechanisms
  • Vibrio bacteria research studies
  • Polyoxometalates: Synthesis and Applications
  • Gout, Hyperuricemia, Uric Acid
  • Glutathione Transferases and Polymorphisms
  • Hemoglobinopathies and Related Disorders
  • Peroxisome Proliferator-Activated Receptors

The University of Queensland
2021-2025

Kiel University
2021-2024

Background: Mutations in the gene MTARC1 (mitochondrial amidoxime–reducing component 1) protect carriers from metabolic dysfunction–associated steatohepatitis (MASH) and cirrhosis. encodes mARC1 enzyme, which is localized to mitochondria has no known MASH-relevant molecular function. Our studies aimed expand on published human genetic data observe effects of modulation preclinical MASH models. Methods Results: We identified a novel structural variant deletion MTARC1, associated with various...

10.1097/hc9.0000000000000365 article EN cc-by-nc-nd Hepatology Communications 2024-04-12

ABSTRACT Sulfoxide reductases in pathogenic bacteria have recently received increasing attention for their association with virulence and survival within the host. Here, we re-investigated physiological role of molybdenum-containing DmsABC dimethyl sulfoxide (DMSO) reductase from Escherichia coli , which has a proposed anaerobic respiration DMSO. Our investigation into potential substrates revealed that efficiently reduces pyrimidine N-oxide, nicotinamide methionine sulfoxide, exposure to...

10.1128/jb.00463-24 article EN cc-by Journal of Bacteriology 2025-03-31

Lysozymes are an essential part of nutrition and antibacterial immunity in metazoans, executing the breakdown bacterial cell walls via hydrolysis peptidoglycan. Although various lysozymes have been reported for several bilaterian phyla, origin metazoan remains elusive as they seem to be lacking non-bilaterian animals. In this study, we investigated a putative goose-type lysozyme (PLys, glycoside hydrolase family 23, GH23) placozoan Trichoplax sp. H2 which localized gland cells ventral...

10.1101/2024.10.06.616844 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-10-06

X-ray absorption near-edge structure (XANES) and extended fine (EXAFS) data have been used to characterize the coordination environment for catalytic Mo site of

10.1021/acs.inorgchem.3c00342 article EN Inorganic Chemistry 2023-03-27

The mitochondrial amidoxime reducing component (mARC) is a human molybdoenzyme known to catalyze the reduction of various N-oxygenated substrates. physiological function mARC enzymes, however, remains unknown. In this study, we examine hydrogen peroxide (H2O2) by mARC1 and mARC2 enzymes. Furthermore, demonstrate an increased sensitivity toward H2O2 for HEK-293T cells with MTARC1 knockout, which implies role enzymes in cellular response oxidative stress. reactive oxygen species (ROS) formed...

10.3390/molecules28176384 article EN cc-by Molecules 2023-08-31

MtsZ is a molybdenum-containing methionine sulfoxide reductase that supports virulence in the human respiratory pathogen Haemophilus influenzae (Hi). HiMtsZ belongs to group of structurally and spectroscopically uncharacterized S-/N-oxide reductases, all which are found bacterial pathogens. Here, we have solved crystal structure HiMtsZ, reveals substrate-binding site encompasses previously unrecognized part accommodates side chain via interaction with His182 Arg166. Charge amino acid...

10.1016/j.jbc.2021.100672 article EN cc-by-nc-nd Journal of Biological Chemistry 2021-01-01

Human mitochondrial amidoxime reducing component 1 and 2 (mARC1 mARC2) were immobilised on glassy carbon electrodes using the crosslinker glutaraldehyde. Voltammetry was performed in presence of artificial electron transfer mediator methyl viologen, whose redox potential lies negative enzymes’ MoVI/V MoV/IV potentials which determined from optical spectroelectrochemical EPR measurements. Apparent Michaelis constants obtained catalytic limiting currents at various substrate concentrations...

10.1021/acs.analchem.2c02232 article EN Analytical Chemistry 2022-06-14

The mitochondrial amidoxime-reducing component (mARC) is one of the simplest molybdenum-containing enzymes. mARC among a few known reducing enzymes playing an important role in drug metabolism mammals. Here, assay based on fluorescence NADH reported for rapid detection substrates and potential inhibitors mARC. So far unknown might be useful development drugs assigned to nonalcoholic fatty liver disease (NAFLD) similar diseases. Kinetics reactions catalyzed by can recorded with high...

10.1021/acs.analchem.3c02109 article EN Analytical Chemistry 2023-08-07

Recent genome-wide association studies (GWAS) have shown a common variant of the mARC1 protein to be associated with liver disease. Herein, we present crystal structure this p.Ala165Thr at near-atomic resolution. No relevant differences between wild type and are detected.

10.1101/2022.03.26.485076 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-03-28

A combination of X-ray absorption and low-temperature electronic spectroscopies has been used to probe the geometric structures human mitochondrial amidoxime reducing component enzyme (hmARC1) in oxidized Mo(VI) reduced Mo(IV) forms. Extended fine structure analysis revealed that possesses a 5-coordinate [MoO

10.1021/acs.inorgchem.4c02157 article EN Inorganic Chemistry 2024-09-30

N-Hydroxyurea has been known since the 1960s as an antiproliferative drug and is used both in oncology for treatment of hematological disorders such sickle cell anemia where very high daily doses are administered. It assumed that cellular effect N-hydroxyurea caused by inhibition ribonucleotide reductase, while alternative mechanisms, e.g., generation nitric oxide, have also proposed. Despite its many therapeutic applications, metabolism hydroxyurea largely unexplored. The major elimination...

10.1021/acs.jmedchem.4c01148 article EN cc-by Journal of Medicinal Chemistry 2024-10-14
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