Literature DB >> 8021203

Reconstitution of energy-linked activities of the solubilized F1F0 ATP synthase from Bacillus subtilis.

D B Hicks1, D M Cohen, T A Krulwich.   

Abstract

The F1F0 ATP synthases from wild-type Bacillus subtilis and an uncoupler-resistant mutant have comparable subunit structures. In accord with an earlier hypothesis, ATP hydrolysis and ATP-Pi exchange by the two synthases were equally stimulated and inhibited by protonophores, respectively, when reconstituted alone in either wild-type or mutant lipids.

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Year:  1994        PMID： 8021203      PMCID： PMC205623          DOI： 10.1128/jb.176.13.4192-4195.1994

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  17 in total

1.  A convenient method for the ATPase assay.

Authors:  D LeBel; G G Poirier; A R Beaudoin
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2.  Reconstitution, a way of biochemical research; some new approaches to membrane-bound enzymes.

Authors:  E Racker; B Violand; S O'Neal; M Alfonzo; J Telford
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3.  Mutants of Bacillus species isolated on the basis of protonophore resistance are deficient in fatty acid desaturase activity.

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4.  Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

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5.  Preparation and reconstitution of F1F0 and F0 from Escherichia coli.

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8.  Purification and reconstitution of the F1F0-ATP synthase from alkaliphilic Bacillus firmus OF4. Evidence that the enzyme translocates H+ but not Na+.

Authors:  D B Hicks; T A Krulwich
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Authors:  D B Hicks; T A Krulwich
Journal:  J Biol Chem       Date:  1986-09-25       Impact factor: 5.157
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