TY - JOUR
T1 - 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
AU - Khananshvili, Daniel
AU - Gromet-Elhanan, Zippora
PY - 1982/9/30
Y1 - 1982/9/30
N2 - The purified, reconstitutively active, β-subunit of the Fo·F1-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.
AB - The purified, reconstitutively active, β-subunit of the Fo·F1-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.
UR - http://www.scopus.com/inward/record.url?scp=0020493980&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(82)90913-5
DO - 10.1016/0006-291X(82)90913-5
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AN - SCOPUS:0020493980
VL - 108
SP - 881
EP - 887
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -