Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Herrick Baltscheffsky"'
Autor:
Bengt Persson, Herrick Baltscheffsky
Publikováno v:
Journal of Molecular Evolution. 78:140-147
A gene for membrane-integral inorganic pyrophosphatase (miPPase) was found in the composite genome of the extremophile archaeon Candidatus Korarchaeum cryptofilum (CKc). This korarchaeal genome shows unusual partial similarity to both major archaeal
Publikováno v:
IUBMB Life. 59:76-83
Suggestions by Calvin about a role of inorganic pyrophosphate (PPi) in early photosynthesis and by Lipmann that PPi may have been the original energy-rich phosphate donor in biological energy conversion, were followed in the mid-1960s by experimental
Publikováno v:
FEBS Letters. 457:527-533
The earliest known H+-PPase (proton-pumping inorganic pyrophosphatase), the integrally membrane-bound H+-PPi synthase (proton-pumping inorganic pyrophosphate synthase) from Rhodospirillum rubrum, is still the only alternative to H+-ATP synthase in bi
Autor:
N. Holm, Herrick Baltscheffsky
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817
Autor:
Nils G. Holm, Herrick Baltscheffsky
Publikováno v:
Origins of Life and Evolution of the Biosphere
The discovery that photosynthetic bacterial membrane-bound inorganic pyrophosphatase (PPase) catalyzed light-induced phosphorylation of orthophosphate (Pi) to pyrophosphate (PPi) and the capability of PPi to drive energy requiring dark reactions supp
Publikováno v:
Biochemical and Biophysical Research Communications. 186:122-128
The yeast Saccharomyces cerevisiae has two inorganic pyrophosphatases that are structurally related. One, PPA1, is a cytoplasmic enzyme. The other, PPA2, is located in the mitochondria and appears to be energy-linked. The sequence similarity of PPA1
Autor:
Sushama W. Deopujari, Lucia Pereira da Silva, Lidia Lichko, Herrick Baltscheffsky, Maria Lundin
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1098:217-223
We have studied a mitochondrial inorganic pyrophosphatase (PPase) in the yeast Saccharomyces cerevisiae. The uncoupler FCCP (carbonyl cyanide p-trifluoromethoxyphenylhydrazone) and the ionophores valinomycin and nigericin stimulate the PPase activity
Publikováno v:
The FEBS journal. 273(22)
The unique family of membrane-bound proton-pumping inorganic pyrophosphatases, involving pyrophosphate as the alternative to ATP, was investigated by characterizing 166 members of the UniProtKB/Swiss-Prot + UniProtKB/TrEMBL databases and available co
Publikováno v:
Journal of bioenergetics and biomembranes. 36(1)
Comparative studies between the proton-pumping, membrane-bound inorganic pyrophosphatases (H(+)-PPases) from hyperthermophilic and thermophilic prokaryotes and those from mesophilic organisms can now be performed because of very recent sequence data.