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Purification characterization of the inhibitory subunit (δ) of the ATP‐synthase from Micrococcus luteus
Author(s) -
Grüber Gerhard,
Engelbrecht Siegfried,
Junge Wolfgang,
Dose Klaus,
Nawroth Thomas
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01271-7
Subject(s) - micrococcus luteus , atp synthase , protein subunit , inhibitory postsynaptic potential , chemistry , biochemistry , atp synthase gamma subunit , micrococcus , biology , enzyme , bacteria , escherichia coli , atpase , genetics , gene , atp hydrolysis , endocrinology
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.