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Inhibition of ATP Hydrolysis by Thermoalkaliphilic F(1)F(o)-ATP Synthase Is Controlled by the C Terminus of the ɛ Subunit

The F(1)F(o)-ATP synthases of alkaliphilic bacteria exhibit latent ATPase activity, and for the thermoalkaliphile Bacillus sp. strain TA2.A1, this activity is intrinsic to the F(1) moiety. To study the mechanism of ATPase inhibition, we developed a heterologous expression system in Escherichia coli...

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書誌詳細
主要な著者: Keis, Stefanie, Stocker, Achim, Dimroth, Peter, Cook, Gregory M.
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Microbiology 2006
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC1482892/
https://ncbi.nlm.nih.gov/pubmed/16707672
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.00040-06
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