Abstract:
:An alpha beta heterodimer of the F1-ATPase of Rhodospirillum rubrum was isolated by extraction of chromatophores with LiCl. Each alpha beta heterodimer contains one tightly bound ADP, which is released upon removal of medium Mg2+. The dimer can be reversibly dissociated by removal of Mg(2+)-ions. The alpha beta heterodimer restores both ATP-synthetic and -hydrolytic activities to LiCl-treated chromatophores, saturation being achieved at approximately 2 mmol alpha beta.mol BChl-1. The heterodimer itself hydrolyses Mg-ATP with an activity distinct from RF1, being unaffected by azide or sulphite ions. The Vmax and Km (ATP) for this Mg(2+)-dependent activity were 110 +/- 10 nmol.min-1.mg protein-1 and 100 +/- 30 microM, respectively. The Km did not differ significantly from that of RF1.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Andralojc PJ,Harris DAdoi
10.1016/0014-5793(92)81326-hkeywords:
subject
Has Abstractpub_date
1992-09-28 00:00:00pages
187-92issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(92)81326-Hjournal_volume
310pub_type
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