The interaction of nucleotides with F1-ATPase inactivated with 4-chloro-7-nitrobenzofurazan.
Biochim Biophys Acta
; 635(2): 284-94, 1981 Apr 13.
Article
em En
| MEDLINE
| ID: mdl-6453611
ABSTRACT
In common with the F1-ATPase from other sources, yeast mitochondrial F1-ATPase was inhibited by 4-chloro-7-nitrobenzofurazan. Total inhibition of the F1-ATPase activity was compatible with the modification of a single tyrosine residue per F1-ATPase molecule. Radioactive labelling experiments localized this modification on a beta-subunit. The inactive modified enzyme retained the capacity to bind the photoaffinity label 8-azido-1,N6-etheno-ATP, which has previously been shown to bind nucleotide sites of low affinity. As well, the inactive modified enzyme bound MgATP with high affinity, yielding a Kd of 14 microM. The results are consistent with the hypothesis of alternating, or cooperative, site catalysis by F1-ATPase.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxidiazóis
/
Fosforilação Oxidativa
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Saccharomyces cerevisiae
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Azidas
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Marcadores de Afinidade
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Trifosfato de Adenosina
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Adenosina Trifosfatases
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Etenoadenosina Trifosfato
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4-Cloro-7-nitrobenzofurazano
Idioma:
En
Ano de publicação:
1981
Tipo de documento:
Article