Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Dagmar Rother"'
Publikováno v:
Microbiology. 154:1980-1988
The periplasmic thiol-disulfide oxidoreductase SoxS is essential for chemotrophic growth of Paracoccus pantotrophus with thiosulfate. To trap its periplasmic partner, the cysteine residues of the CysXaaXaaCys motif of SoxS (11 kDa) were changed to al
Autor:
Christoph Laurich, Dagmar Rother, Edward J. Reijerse, Petra Hellwig, Wolfgang Lubitz, Monika Sommerhalter, Eberhard Bothe, Cornelius G. Friedrich, Armin Quentmeier
Publikováno v:
Biochemistry. 46:7804-7810
The heterodimeric hemoprotein SoxXA, essential for lithotrophic sulfur oxidation of the aerobic bacterium Paracoccus pantotrophus, was examined by a combination of spectroelectrochemistry and EPR spectroscopy. The EPR spectra for SoxXA showed contrib
Autor:
Frank Bardischewsky, Cornelius G. Friedrich, Armin Quentmeier, Dagmar Rother, Grazyna Orawski
Publikováno v:
Microbiology. 153:1081-1086
The significance of the soxS gene product on chemotrophic sulfur oxidation of Paracoccus pantotrophus was investigated. The thioredoxin SoxS was purified, and the N-terminal amino acid sequence identified SoxS as the soxS gene product. The wild-type
Publikováno v:
Microbiology. 151:1707-1716
Paracoccus pantotrophus GB17 requires thiosulfate for induction of the sulfur-oxidizing (Sox) enzyme system. The soxRS genes are divergently oriented to the soxVWXYZA–H genes. soxR predicts a transcriptional regulator of the ArsR family and soxS a
Autor:
Dagmar Rother, Cornelius G. Friedrich
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1598:65-73
The heterodimeric c-type cytochrome complex SoxXA of Paracoccus pantotrophus was produced in Escherichia coli. The soxX and soxA genes, separated by two genes in the sox gene cluster of P. pantotrophus, were fused with ribosome binding sites optimal
Publikováno v:
Biochemistry
Biochemistry, 2011, 50 (1), pp.17-24. ⟨10.1021/bi1013112⟩
Biochemistry, 2011, 50 (1), pp.17-24. ⟨10.1021/bi1013112⟩
PMID: 21110519; A new way to study the electrochemical properties of proteins by coupling front-face fluorescence spectroscopy with an optically transparent thin-layer electrochemical cell is presented. First, the approach was examined on the basis o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cf39ee2e6554f2fa570a8bb002fb9b1
https://hal.archives-ouvertes.fr/hal-03332607
https://hal.archives-ouvertes.fr/hal-03332607
Autor:
Armin Quentmeier, Cornelius G. Friedrich, Dagmar Rother, Eduard J. Reijerse, Wolfgang Lubitz, Simon C. Drew
Publikováno v:
Inorganic chemistry. 50(2)
The bacterial sulfane dehydrogenase SoxCD is a distantly related member of the sulfite oxidase (SO) enzyme family that is proposed to oxidize protein-bound sulfide (sulfane) of SoxY as part of a multienzyme mechanism of thiosulfate metabolism. This s
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 65(Pt 3)
The periplasmic thiol-disulfide oxidoreductase SoxS is beneficial for the sulfur-oxidizing (Sox) phenotype of the facultative chemotrophic bacterium Paracoccus pantotrophus and is not part of the Sox enzyme system. SoxS combines features of thioredox
Autor:
Jürg Fischer, Dagmar Rother, Grazyna Orawski, Cornelius G. Friedrich, Frank Bardischewsky, Petra Hellwig, Armin Quentmeier
Publikováno v:
Microbial Sulfur Metabolism ISBN: 9783540726791
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a1a755767389cf6064ab1666910d636
https://doi.org/10.1007/978-3-540-72682-1_12
https://doi.org/10.1007/978-3-540-72682-1_12
Publikováno v:
GBM Annual Spring meeting Mosbach 2006. 2006