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

doi:10.1042/ba20030132

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 journal › Article › peer-review

4 Scopus citations

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 P_i 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 language	English (US)
Pages (from-to)	293-301
Number of pages	9
Journal	Biotechnology and Applied Biochemistry
Volume	39
Issue number	3
DOIs	https://doi.org/10.1042/ba20030132
State	Published - Jun 2004
Externally published	Yes

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

Access to Document

10.1042/ba20030132

Cite this

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

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.",

keywords = "ATP synthesis, Bacterial FF-ATPase, Biotin tag, Energy transduction, Immobilization, Uniform orientation",

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AU - Schiavone, Marc

AU - Nayak, Amiya

AU - Bhattacharya, Sanjoy K.

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AB - 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.

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KW - Energy transduction

KW - Immobilization

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