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The DCCD-reactive aspartyl-residue of subunit C from the Escherichia coli ATP-synthase is important for the conformation of F0.

Abstract：

:The effect of various point mutations in subunits a and and c of the E. coli ATP-synthase was characterized. In each of the mutants there was no F0-dependent H+-conduction, but still an ATPase-activity comparable to wildtype activities. In addition, the subunit b could be extracted from the mutant's F0 but not from the F0 of wildtype. The effects are interpreted as a change in the conformation of F0 caused by the different mutations.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Friedl P,Hoppe J,Schairer HU

doi

10.1016/0006-291x(84)91286-5

subject

Has Abstract

pub_date

1984-04-30 00:00:00

pages

527-33

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)91286-5

journal_volume

120

pub_type

杂志文章

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