Literature DB >> 2529907

Immunoelectron microscopic localization of the F1F0 ATPase (ATP synthase) on the cytoplasmic membrane of alkalophilic Bacillus firmus RAB.

M Rohde1, F Mayer, D B Hicks, T A Krulwich.   

Abstract

Evidence that the F1F0 ATPase (ATP synthase) of alkalophilic Bacillus firmus RAB is localized exclusively on the cytoplasmic membrane was obtained by immunogold electron microscopy using a highly specific polyclonal antibody against the beta subunit of Escherichia coli F1F0 ATPase. The energetic problem faced by cells of B. firmus RAB growing oxidatively at pH 10.5 despite a low protonmotive force across the cytoplasmic membrane cannot, therefore, be circumvented by localization of energy transducing functions on hypothetical internal membranes.

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Year:  1989        PMID: 2529907     DOI: 10.1016/0005-2736(89)90369-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

Review 1.  Proton-coupled bioenergetic processes in extremely alkaliphilic bacteria.

Authors:  T A Krulwich; A A Guffanti
Journal:  J Bioenerg Biomembr       Date:  1992-12       Impact factor: 2.945

2.  Organization and nucleotide sequence of the atp genes encoding the ATP synthase from alkaliphilic Bacillus firmus OF4.

Authors:  D M Ivey; T A Krulwich
Journal:  Mol Gen Genet       Date:  1991-10

3.  Functional compartmentalization in bacteria and archaea. A hypothetical interface between cytoplasmic membrane and cytoplasm.

Authors:  F Mayer; M Hoppert
Journal:  Naturwissenschaften       Date:  1996-01

4.  Growth and bioenergetics of alkaliphilic Bacillus firmus OF4 in continuous culture at high pH.

Authors:  M G Sturr; A A Guffanti; T A Krulwich
Journal:  J Bacteriol       Date:  1994-06       Impact factor: 3.490

5.  Membrane ultrastructure of alkaliphilic Bacillus species studied by rapid-freeze electron microscopy.

Authors:  S Khan; D M Ivey; T A Krulwich
Journal:  J Bacteriol       Date:  1992-08       Impact factor: 3.490

  5 in total

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