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of 5
pro vyhledávání: '"Richard, Brosi"'
Autor:
Richard Brosi, Ryu-Ryun Kim, Lorenz Heidinger, Robert Bittl, Adelbert Bacher, Stefan Weber, Boris Illarionov, Markus Fischer, Erik Schleicher
Publikováno v:
The journal of physical chemistry. B. 124(9)
Flavin semiquinones are common intermediate redox states in flavoproteins, and thus, knowledge of their electronic structure is essential for fully understanding their chemistry and chemical versatility. In this contribution, we use a combination of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf7871eb1618f3623d991593d5dac1db
https://pubmed.ncbi.nlm.nih.gov/32011886
https://pubmed.ncbi.nlm.nih.gov/32011886
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1146
Flavoproteins often employ radical mechanisms in their enzymatic reactions. This involves paramagnetic species, which can ideally be investigated with electron paramagnetic resonance (EPR) spectroscopy. In this chapter we focus on the example of flav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::081218fa74a21c6be411796611bacdd5
https://pubmed.ncbi.nlm.nih.gov/24764097
https://pubmed.ncbi.nlm.nih.gov/24764097
Publikováno v:
Methods in Molecular Biology ISBN: 9781493904518
Flavoproteins often employ radical mechanisms in their enzymatic reactions. This involves paramagnetic species, which can ideally be investigated with electron paramagnetic resonance (EPR) spectroscopy. In this chapter we focus on the example of flav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fe990d813fbd8405305fefe050054af2
https://doi.org/10.1007/978-1-4939-0452-5_13
https://doi.org/10.1007/978-1-4939-0452-5_13
Autor:
Ralf Seidel, Anna Scherer, Richard Brosi, Andrea Steinmetz, Ilme Schlichting, Thorsten Lorenz, Jochen Reinstein, Robert Bittl, Elisabeth Hartmann, Thomas R. M. Barends, Sabine Zimmermann, Robert L. Shoeman, Jessica Eschenbach
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
The crystal structure of the N-terminal part of T. thermophilus DnaJ unexpectedly showed an ordered GF domain and guided the design of a construct enabling the first structure determination of a complete DnaJ cochaperone molecule. By combining the cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7091beb79d6c04de29138f41db0b40cd
https://pubmed.ncbi.nlm.nih.gov/23897477
https://pubmed.ncbi.nlm.nih.gov/23897477
Autor:
Tilo Mathes, Richard Brosi, Monika Joshi, Markus Fischer, Stefan Weber, Peter Hegemann, Robert Bittl, Adelbert Bacher, Boris Illarionov, Erik Schleicher
Publikováno v:
Journal of the American Chemical Society. 132(26)
Exploring protein-cofactor interactions on a molecular level is one of the major challenges in modern biophysics. Based on structural data alone it is rarely possible to identify how subtle interactions between a protein and its cofactor modulate the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::943d7f90c3312ae77ac661871b485f39
https://pubmed.ncbi.nlm.nih.gov/20536240
https://pubmed.ncbi.nlm.nih.gov/20536240