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

Abstract:

:The immobilization of F(0)F(1)-ATPase in uniform orientation is reported. The biotinylated and histidine-tagged subunits of the bacterial F(0)F(1)-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.

authors

Bhattacharya S,Schiavone M,Nayak A,Bhattacharya SK

doi

10.1042/BA20030132

subject

Has Abstract

pub_date

2004-06-01 00:00:00

pages

293-301

issue

Pt 3

eissn

0885-4513

issn

1470-8744

pii

BA20030132

journal_volume

39

pub_type

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