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Chemical modification of the β-subunit isolated from a membrane-bound Fo·F1-ATP synthase:Modification by 4-chloro-7-nitrobenzofurazan does not inhibit restoration of ATP synthesis or hydrolysis

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
108
Issue
2
Identifiers
DOI: 10.1016/0006-291x(82)90913-5

Abstract

Abstract The purified, reconstitutively active, β-subunit of the Fo·F 1-ATP synthase of Rhodospirillum rubrum chromatophores was found to bind both 4-chloro-7-nitrobenzofurazan (NBD-Cl) and dicyclohexylcarbodiimide (DCCD). The binding stoichiometry at saturation was 1 mol of either reagent per mol of β. The NBD-modified β-subunit did rebind to the β-less chromatophores and restored all their lost ATP-linked activities as efficiently as the untreated β, whereas the DCCD-modified β-subunit lost completely its capacity to rebind to the depleted chromatophores. These results suggest that the amino acid residue which is modified by NBD-Cl in the isolated β-subunit is not essential for binding and may be also not for activity.

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