In:
FEBS Letters, Wiley, Vol. 356, No. 2-3 ( 1994-12-19), p. 226-228
Abstract:
Subunit δ was isolated from the ATP‐synthase from Micrococcus luteus strain (ATCC 4698). δ, in the case of M. luteus F 0 F 1 ‐ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP‐synthase. After treatment with 1.5 M LiCl the ATP‐synthase dissociated, and subsequently subunit δ (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP‐synthase lacking δ by addition of δ showed noncompetitive kinetics with a K i of ∼ 5.9nM. Subunit ε from chloroplast F 1 , which corresponds functionally to the M. luteus F 0 F 1 ‐δ, and chloroplast δ were tested for ATPase inhibitory activity by addition to the partially δ‐depleted ATP‐synthase from M. luteus . CF 1 ‐ε inhibited M. luteus ATP‐synthase up to 80%, whereas CF 1 ‐δ did not show any influence.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(94)01271-7
Language:
English
Publisher:
Wiley
Publication Date:
1994
detail.hit.zdb_id:
1460391-3
SSG:
12