Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Roland Groß"'
Publikováno v:
Chemical Engineering & Technology. 43:904-912
Publikováno v:
Surface and Coatings Technology. 316:219-225
The copper wall of regeneratively cooled liquid fuel rocket-combustion chambers is exposed to high thermomechanical loads. Although it is cooled by liquid hydrogen in internal cooling channels, surface temperatures of more than 800 °C on the hot-gas
Autor:
Florian Schiemann, Frank Petersen, Jessica Mittelstädt, Ernst Brandt, Roland Gross, Buko Lindner, Jan Schulmistrat, Christian P. Sommerhoff
Publikováno v:
The Journal of Immunology. 183:2223-2231
The cathelicidin LL-37 represents a potent antimicrobial and cell-stimulating agent, most abundantly expressed in peripheral organs such as lung and skin during inflammation. Because mast cells (MC) overtake prominent immunomodulatory roles in these
Autor:
Ursula S. Sauer, Alexander H. Haas, Roland Gross, C. Roy D. Lancaster, Jörg Simon, Werner Mäntele
Publikováno v:
Biochemistry. 44:13949-13961
Electrochemically induced static FTIR difference spectroscopy has been employed to investigate redox-driven protonation changes of individual amino acid residues in the quinol:fumarate reductase (QFR) from Wolinella succinogenes. The difference spect
Publikováno v:
Molecular Microbiology. 49:69-79
The rumen bacterium Wolinella succinogenes grows by respiratory nitrate ammonification with formate as electron donor. Whereas the enzymology and coupling mechanism of nitrite respiration is well known, nitrate reduction to nitrite has not yet been e
Publikováno v:
FEBS Letters. 522:83-87
The two multiheme c-type cytochromes NrfH and NrfA form a membrane-bound complex that catalyzes menaquinol oxidation by nitrite during respiratory nitrite ammonification of Wolinella succinogenes. Each cysteine residue of the four NrfH heme c binding
Publikováno v:
Molecular Microbiology. 35:686-696
Wolinella succinogenes can grow by anaerobic respiration with nitrate or nitrite using formate as electron donor. Two forms of nitrite reductase were isolated from the membrane fraction of W. succinogenes. One form consisted of a 58 kDa polypeptide (
Publikováno v:
European Journal of Biochemistry. 269:1974-1983
Hydrogenase and fumarate reductase isolated from Wolinella succinogenes were incorporated into liposomes containing menaquinone. The two enzymes were found to be oriented solely to the outside of the resulting proteoliposomes. The proteoliposomes cat
Publikováno v:
European Journal of Biochemistry. 268:5776-5782
The electron-transport chain that catalyzes nitrite respiration with formate in Wolinella succinogenes consists of formate dehydrogenase, menaquinone and the nitrite reductase complex. The latter catalyzes nitrite reduction by menaquinol and is made
Publikováno v:
Archives of Microbiology. 176:310-313
The cell homogenate and the soluble cell fraction of Wolinella succinogenes grown with formate and fumarate catalyzed the oxidation of benzyl viologen radical by methacrylate [apparent Km=0.23 mM, Vmax=1.0 U (mg cell protein) -1] or acrylate [apparen