Application of thermostable reaction centers from Chloroflexus aurantiacus as a protonmotive force generating system
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منابع مشابه
Electronic pathway in reaction centers from Rhodobacter sphaeroides and Chloroflexus aurantiacus.
The reaction centers (RC) of Chloroflexus aurantiacus and Rhodobacter sphaeroidesH(M182)L mutant were investigated. Prediction for electron transfer (ET) at very low temperatures was also performed. To describe the kinetics of the C. aurantiacus RCs, the incoherent model of electron transfer was used. It was shown that the asymmetry in electronic coupling parameters must be included to explain ...
متن کاملA bicyclic autotrophic CO2 fixation pathway in Chloroflexus aurantiacus.
Phototrophic CO(2) assimilation by the primitive, green eubacterium Chloroflexus aurantiacus has been shown earlier to proceed in a cyclic mode via 3-hydroxypropionate, propionyl-CoA, succinyl-CoA, and malyl-CoA. The metabolic cycle could be closed by cleavage of malyl-CoA affording glyoxylate (the primary CO(2) fixation product) with regeneration of acetyl-CoA serving as the starter unit of th...
متن کاملSANS investigation of the photosynthetic machinery of Chloroflexus aurantiacus.
Green photosynthetic bacteria harvest light and perform photosynthesis in low-light environments, and contain specialized antenna complexes to adapt to this condition. We performed small-angle neutron scattering (SANS) studies to obtain structural information about the photosynthetic apparatus, including the peripheral light-harvesting chlorosome complex, the integral membrane light-harvesting ...
متن کاملRole of the AcsF protein in Chloroflexus aurantiacus.
The green phototrophic bacteria contain a unique complement of chlorophyll pigments, which self-assemble efficiently into antenna structures known as chlorosomes with little involvement of protein. The few proteins found in chlorosomes have previously been thought to have a primarily structural function. The biosynthetic pathway of the chlorosome pigments, bacteriochlorophylls c, d, and e, is n...
متن کاملPurification and Properties of a Maltotetraose- and Maltotriose-Producing Amylase from Chloroflexus aurantiacus.
A maltotetraose- and maltotriose-producing amylase which is stable at alkaline pHs and high temperatures was detected in the culture filtrate of a strain of Chloroflexus aurantiacus J-10-F1, a thermophilic, green, photosynthetic bacterium. The enzyme was purified to homogeneity, as demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by means of ultrafiltration, ammonium s...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 1993
ISSN: 0005-2728
DOI: 10.1016/0005-2728(93)90155-9