Uniformly oriented bacterial F0F1-ATPase immobilized on a semi-permeable membrane: A step towards biotechnological energy transduction

Sumana Bhattacharya, Marc Schiavone, Amiya Nayak, Sanjoy K Bhattacharya

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The immobilization of F0F1-ATPase in uniform orientation is reported. The biotinylated and histidine-tagged subunits of the bacterial F0F1-ATPase complex were used for immobilization of the complex on artificial semi-permeable membranes resulting in 88 ± 7.8 and 72 ± 5.2% coupling of the enzymes. The immobilized enzymes retained over 90% activity. The immobilized ATPase/synthase was used for generation of ATP from ADP and Pi at the expense of electrochemical potential energy. The re-usability, ratio of amount of enzyme immobilized to enzymic activity conferred on the membranes, ATP synthesized by assembled system and suitability of ATP generated for use in coupled enzymic reactions were determined.

Original languageEnglish
Pages (from-to)293-301
Number of pages9
JournalBiotechnology and Applied Biochemistry
Volume39
Issue number3
StatePublished - Jun 1 2004
Externally publishedYes

Fingerprint

Proton-Translocating ATPases
Adenosinetriphosphate
Immobilized Enzymes
Enzymes
Adenosine Triphosphate
Membranes
Immobilization
Administrative data processing
Reusability
Potential energy
Histidine
Adenosine Diphosphate
Adenosine Triphosphatases
Catalyst activity

Keywords

  • ATP synthesis
  • Bacterial FF-ATPase
  • Biotin tag
  • Energy transduction
  • Immobilization
  • Uniform orientation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology

Cite this

Uniformly oriented bacterial F0F1-ATPase immobilized on a semi-permeable membrane : A step towards biotechnological energy transduction. / Bhattacharya, Sumana; Schiavone, Marc; Nayak, Amiya; Bhattacharya, Sanjoy K.

In: Biotechnology and Applied Biochemistry, Vol. 39, No. 3, 01.06.2004, p. 293-301.

Research output: Contribution to journalArticle

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