TY  - GEN
A1  - Abbas, Ioana M.
A1  - Vranic, Marija
A1  - Hoffmann, Holger
A1  - El-Khatib, Ahmed H.
A1  - Montes-Bayón, María
A1  - Möller, Heiko Michael
A1  - Weller, Michael G.
T1  - Investigations of the Copper Peptide Hepcidin-25 by
LC-MS/MS and NMR⁺
T2  - Postprints der Universität Potsdam Mathematisch-Naturwissenschaftliche Reihe
N2  - Hepcidin-25 was identified as themain iron regulator in the human body, and it by binds to the sole iron-exporter ferroportin. Studies showed that the N-terminus of hepcidin is responsible for this interaction, the same N-terminus that encompasses a small copper(II) binding site known as the ATCUN (amino-terminal Cu(II)- and Ni(II)-binding) motif. Interestingly, this copper-binding property is largely ignored in most papers dealing with hepcidin-25. In this context, detailed investigations of the complex formed between hepcidin-25 and copper could reveal insight into its biological role. The present work focuses on metal-bound hepcidin-25 that can be considered the biologically active form. The first part is devoted to the reversed-phase chromatographic separation of copper-bound and copper-free hepcidin-25 achieved by applying basic mobile phases containing 0.1% ammonia. Further, mass spectrometry (tandemmass spectrometry (MS/MS), high-resolutionmass spectrometry (HRMS)) and nuclear magnetic resonance (NMR) spectroscopy were employed to characterize the copper-peptide. Lastly, a three-dimensional (3D)model of hepcidin-25with bound copper(II) is presented. The identification of metal complexes and potential isoforms and isomers, from which the latter usually are left undetected by mass spectrometry, led to the conclusion that complementary analytical methods are needed to characterize a peptide calibrant or referencematerial comprehensively. Quantitative nuclear magnetic resonance (qNMR), inductively-coupled plasma mass spectrometry (ICP-MS), ion-mobility spectrometry (IMS) and chiral amino acid analysis (AAA) should be considered among others.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 701 
KW  - hepcidin-25
KW  - copper
KW  - nickel
KW  - copper complex
KW  - ATCUN motif
KW  - metal complex
KW  - MS
KW  - NMR structure
KW  - metal peptide
KW  - metalloprotein
KW  - metallopeptide
KW  - isomerization
KW  - racemization
KW  - purity
KW  - reference material
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-427926
SN  - 1866-8372
IS  - 701
ER  - 
TY  - JOUR
A1  - Toulouse, Charlotte Marguerite
A1  - Schmucker, Sonja
A1  - Metesch, Kristina
A1  - Pfannstiel, Jens
A1  - Michel, Bernd
A1  - Starke, Ines
A1  - Möller, Heiko Michael
A1  - Stefanski, Volker
A1  - Steuber, Julia
T1  - Mechanism and impact of catecholamine conversion by Vibrio cholerae
JF  - Biochimica et biophysica acta : Bioenergetics
N2  - Bacterial pathogens are influenced by signaling molecules including the catecholamines adrenaline and noradrenaline which are host-derived hormones and neurotransmitters. Adrenaline and noradrenaline modulate growth, motility and virulence of bacteria. We show that adrenaline is converted by the pathogen Vibrio cholerae to adrenochrome in the course of respiration, and demonstrate that superoxide produced by the respiratory, Na+ - translocating NADH:quinone oxidoreductase (NQR) acts as electron acceptor in the oxidative conversion of adrenaline to adrenochrome. Adrenochrome stimulates growth of V. cholerae, and triggers specific responses in V. cholerae and in immune cells. We performed a quantitative proteome analysis of V. cholerae grown in minimal medium with glucose as carbon source without catecholamines, or with adrenaline, noradrenaline or adrenochrome. Significant regulation of proteins participating in iron transport and iron homeostasis, in energy metabolism, and in signaling was observed upon exposure to adrenaline, noradrenaline or adrenochrome. On the host side, adrenochrome inhibited lipopolysaccharide-triggered formation of TNF-alpha by THP-1 monocytes, though to a lesser extent than adrenaline. It is proposed that adrenochrome produced from adrenaline by respiring V. cholerae functions as effector molecule in pathogen-host interaction.
KW  - Vibrio cholerae
KW  - Na+ - NADH:quinone oxidoreductase
KW  - NQR
KW  - Superoxide
KW  - Adrenaline
KW  - Adrenochrome
Y1  - 2019
U6  - https://doi.org/10.1016/j.bbabio.2019.04.003
SN  - 0005-2728
SN  - 1879-2650
VL  - 1860
IS  - 6
SP  - 478
EP  - 487
PB  - Elsevier
CY  - Amsterdam
ER  -