About: Petra Hellwig

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher

Attributes	Values
rdf:type	Item
description	forskare (sv) ikertzailea (eu) исследовательница (ru) researcher (en) 연구원 (ko) গবেষক (bn) 研究者 (ja) araştırmacı (tr) дослідниця (uk) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) scheikundige (nl) հետազոտող (hy) hulumtuese (sq) ricercatrice (it)
rdfs:label	Petra Hellwig (en) Petra Hellwig (es) Petra Hellwig (fr) Petra Hellwig (nl) Petra Hellwig (sl) Petra Hellwig (sq) Petra Hellwig (ast)
skos:prefLabel	Petra Hellwig (en) Petra Hellwig (es) Petra Hellwig (fr) Petra Hellwig (nl) Petra Hellwig (sl) Petra Hellwig (sq) Petra Hellwig (ast)
name	Petra Hellwig (en) Petra Hellwig (es) Petra Hellwig (fr) Petra Hellwig (nl) Petra Hellwig (sl) Petra Hellwig (sq) Petra Hellwig (ast)
Scopus author ID	wds:Q42838298-080D168B-0E6F-424D-910D-9926458686EC
Scopus author ID	7003601343
given name	wds:Q42838298-A61D792E-918D-46A2-AAC2-BA2B339FE47E
given name	Petra
instance of	wds:Q42838298-83F90863-7DCE-4BA8-9BF7-010F77F684DD
instance of	Homo sapiens
Loop ID	wds:Q42838298-9115A139-B44B-4694-85B0-56C8DE4CF081
Loop ID	241689
doctoral student	wds:Q42838298-E989D3CE-D465-442B-A78B-1A37D6101D3B
doctoral student	Youssef El Khoury
IUF member ID	wds:Q42838298-85137348-F5F4-4E73-8E6C-AF66B8481D69
IUF member ID	1154
Theses.fr person ID	wds:Q42838298-EBAA95CD-4F29-4583-93C5-094022436AFB
Theses.fr person ID	http://www.theses.fr/14269746X/id
Theses.fr person ID	14269746X
occupation	wds:Q42838298-2AED6CE0-A320-4821-9A87-4F3ED88F00F7 wds:Q42838298-5DB300EA-D437-4F06-AEED-A8AB815F317D
employer	wds:Q42838298-6536B9AE-F4F8-4C9F-AF42-1E6418933143
sex or gender	wds:Q42838298-5CFF8993-AE81-4F84-BCC4-4B6FD8C36A87
VIAF ID	wds:Q42838298-38A8EE8D-FAB1-4B49-BF26-935997A5BABC
GND ID	wds:Q42838298-16DC2EAC-53F7-4F1C-A8CA-3513372F248A
IdRef ID	wds:Q42838298-315BCCB5-CBEB-42A3-B527-49E2A2CF7A89
member of	wds:Q42838298-A41B231B-1179-4806-BEC3-2A5FED556DED
date of birth	wds:Q42838298-DC18479C-8247-4900-981E-DD3D94B19051
family name	wds:Q42838298-580053EE-F618-42CD-92C1-BB67EF46ED4F
WorldCat Identities ID (superseded)	wds:Q42838298-5A289934-33E8-4A7D-925A-E6F026B2D29E
VIAF ID	http://viaf.org/viaf/35279203
GND ID	https://d-nb.info/gnd/120116219
IdRef ID	http://www.idref.fr/14269746X/id
occupation	researcher chemist
employer	University of Strasbourg
sex or gender	female organism
VIAF ID	35279203
GND ID	120116219
IdRef ID	14269746X
member of	Institut universitaire de France
date of birth	1970-01-01 00:00:00Z (xsd:dateTime)
family name	Hellwig
WorldCat Identities ID (superseded)	viaf-35279203
ORCID iD	wds:Q42838298-BD080E01-B448-4584-860A-80E753213371
ORCID iD	https://orcid.org/0000-0001-6294-5163
ORCID iD	0000-0001-6294-5163
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42838298
is author of	Spectroscopic analysis of tyrosine derivatives: on the role of the tyrosine-histidine covalent linkage in cytochrome c oxidase Steady-state and time resolved fluorescence analysis on tyrosine-histidine model compounds Site-directed mutation of the highly conserved region near the Q-loop of the cytochrome bd quinol oxidase from Escherichia coli specifically perturbs heme b595. Role of phospholipids in respiratory cytochrome bc(1) complex catalysis and supercomplex formation Probing the Paracoccus denitrificans cytochrome c(1)-cytochrome c(552) interaction by mutagenesis and fast kinetics Time-Resolved FT-IR Studies on the CO Adduct ofParacoccus denitrificansCytochromecOxidase: Comparison of the Fully Reduced and the Mixed Valence Form† Electrochemical and Ultraviolet/Visible/Infrared Spectroscopic Analysis of Hemeaanda3Redox Reactions in the CytochromecOxidase fromParacoccus denitrificans: Separation of Hemeaanda3Contributions and Assignment of Vibrational Modes† Electrochemical, FTIR, and UV/VIS Spectroscopic Properties of theba3Oxidase fromThermus thermophilus† Zinc inhibition of bacterial cytochrome bc(1) reveals the role of cytochrome b E295 in proton release at the Q(o) site Mutational Analysis of Cytochrome b at the Ubiquinol Oxidation Site of Yeast Complex III Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase Redox Dependent Changes at the Heme Propionates in CytochromecOxidase fromParacoccusdenitrificans: Direct Evidence from FTIR Difference Spectroscopy in Combination with Heme Propionate13C Labeling† The Unusal Redox Centers of SoxXA, a Novelc-Type Heme-Enzyme Essential for Chemotrophic Sulfur-Oxidation ofParacoccus pantotrophus† Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† Electrochemically induced FT-IR difference spectra of the two- and four-subunit cytochrome c oxidase from P. denitrificans reveal identical conformational changes upon redox transitions Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae

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