Voltage-dependent absorbance change of carotenoids in halophilic archaebacteria
نویسندگان
چکیده
منابع مشابه
Dihydrolipoamide dehydrogenase from halophilic archaebacteria.
Dihydrolipoamide dehydrogenase has been discovered in the halophilic archaebacteria for the first time. The enzyme from both classical and alkaliphilic halobacteria has been investigated. (1) The enzyme specifically catalysed the stoichiometric oxidation of dihydrolipoamide by NAD+. Enzymic activity was optimal at 2 M-NaCl and was remarkably resistant to thermal denaturation. (2) The relative m...
متن کاملIdentification of carotenoids from the extremely halophilic archaeon Haloarcula japonica
The carotenoids produced by extremely halophilic archaeon Haloarcula japonica were extracted and identified by their chemical, chromatographic, and spectroscopic characteristics (UV-Vis and mass spectrometry). The composition (mol%) was 68.1% bacterioruberin, 22.5% monoanhydrobacterioruberin, 9.3% bisanhydrobacterioruberin, <0.1% isopentenyldehydrorhodopin, and trace amounts of lycopene and phy...
متن کاملProperties of the Plasma Membrane ATPases of the Halophilic Archaebacteria Haloferax mediterranei and Haloferax volcanii
Both, Haloferax mediterranei and Haloferax volcanii membranes contain ATPases which are capable of hydrolyzing ATP in presence of Mg2+ or Mn2+. The ATPases require high con centrations of NaCl, a pH value of 9, and high temperatures up to 60 °C. Free manganese ions inhibited the enzyme activity of either ATPase. The ATPases of Hf. mediterranei and Hf. vol canii, respectively, show different s...
متن کاملTranssulfuration in archaebacteria.
The transfer of sulfur from methionine to cysteine in the archaebacteria Sulfolobus acidocaldarius and Halobacterium marismortui was studied by feeding 34S-labeled methionine to cells and measuring the incorporation of 34S into protein-bound cellular cysteine and methionine by mass spectrometry. It was found that, as are eucaryotes, both of these archaebacteria were able to convert the sulfur o...
متن کاملEstimating the voltage-dependent free energy change of ion channels using the median voltage for activation
Voltage-gated ion channels are crucial for electrical activity and chemical signaling in a variety of cell types. Structure-activity studies involving electrophysiological characterization of mutants are widely used and allow us to quickly realize the energetic effects of a mutation by measuring macroscopic currents and fitting the observed voltage dependence of conductance to a Boltzmann equat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 1996
ISSN: 0005-2736
DOI: 10.1016/0005-2736(96)00114-9