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Autor:
Olbrich AC; Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Düsseldorf, 40225, Germany., Mielenbrink S; Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Düsseldorf, 40225, Germany., Willers VP; Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Düsseldorf, 40225, Germany., Koschorreck K; Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Düsseldorf, 40225, Germany., Birrell JA; School of Life Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK., Span I; Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Düsseldorf, 40225, Germany.; Bioinorganic Chemistry, Friedrich-Alexander-Universität Erlangen-Nürnberg, Egerlandstr. 1, Erlangen, 91058, Germany., Urlacher VB; Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Düsseldorf, 40225, Germany.
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Nov 14, pp. e202403005. Date of Electronic Publication: 2024 Nov 14.
Publikováno v:
Journal of Inherited Metabolic Disease. 21:195-198
P. Y. JENSEN1,2,*, N. BONANDER2, B. G. KARLSSON2, N. HORN3, Z. TU MER3,4 and O. FARVER1 of Analytical and Pharmaceutical Royal Danish School 1Department Chemistry, T he of of Biochemistry and Biophysics, Pharmacy, Copenhagen, Denmark ; 2Department
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c1da3026fdb72700cdfdcbb8319ae412
https://doi.org/10.1023/a:1005331130245
https://doi.org/10.1023/a:1005331130245
Autor:
O. Farver, Israel Pecht
Publikováno v:
Biophysical Chemistry. 50:203-216
Intramolecular long-range electron transfer (ET) processes have been investigated in two types of blue copper proteins; the single-copper protein, azurin and the multi-copper oxidase, ascorbate oxidase. These have several advantages for investigating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3968693a1e8add9ff1a082522d4cf04d
https://doi.org/10.1016/0301-4622(94)85032-1
https://doi.org/10.1016/0301-4622(94)85032-1
Autor:
Bouloukaki, Izolde1 (AUTHOR) izolthi@gmail.com, Christodoulakis, Antonios1,2 (AUTHOR) christodoulakisa@uoc.gr, Margetaki, Katerina1 (AUTHOR) i.tsiligianni@uoc.gr, Tsiligianni, Ioanna1 (AUTHOR)
Publikováno v:
Journal of Clinical Medicine. Aug2024, Vol. 13 Issue 16, p4793. 13p.
Autor:
Ju, Hongyu1,2 (AUTHOR), Cheng, Li2 (AUTHOR), Li, Mengmeng2 (AUTHOR), Mei, Kunrong1 (AUTHOR) kmei@tju.edu.cn, He, Suhang2 (AUTHOR) she@nankai.edu.cn, Jia, Chuancheng2 (AUTHOR) jiacc@nankai.edu.cn, Guo, Xuefeng2,3 (AUTHOR) guoxf@pku.edu.cn
Publikováno v:
Advanced Science. 7/24/2024, Vol. 11 Issue 28, p1-17. 17p.
Publikováno v:
University of Copenhagen
Several amidated biologically active peptides such as pancreastatin, thyrotropin-releasing hormone, pancreatic polypeptide and amylin are produced in endocrine pancreatic tissue which contains the enzyme necessary for their final processing, i.e. pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c34098a19bf26b8338ffa6d883aff25
https://doi.org/10.1042/bj2740739
https://doi.org/10.1042/bj2740739
Publikováno v:
European journal of biochemistry. 267(11)
Azurin contains two potential redox sites, a copper centre and, at the opposite end of the molecule, a cystine disulfide (RSSR). Intramolecular electron transfer between a pulse radiolytically produced RSSR- radical anion and the blue Cu(II) ion was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eca64f3b186d2b8f99abb3a03edf0325
https://pubmed.ncbi.nlm.nih.gov/10824096
https://pubmed.ncbi.nlm.nih.gov/10824096
Publikováno v:
University of Copenhagen
Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was perf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11706573e290d927a5406950fc9da402
https://pubmed.ncbi.nlm.nih.gov/10630893
https://pubmed.ncbi.nlm.nih.gov/10630893
Publikováno v:
European journal of biochemistry. 266(3)
Azide binding to the blue copper oxidases laccase and ascorbate oxidase (AO) was investigated by electron paramagnetic resonance (EPR) and pulsed electron-nuclear double resonance (ENDOR) spectroscopies. As the laccase : azide molar ratio decreases f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::16b46aac536fc3fcb1f33d18f19c7ef2
https://pubmed.ncbi.nlm.nih.gov/10583375
https://pubmed.ncbi.nlm.nih.gov/10583375