大肠杆菌三磷酸腺苷酶β亚基与4-氯-7-硝基苯并呋咱的反应活性 - Suppr

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超能文献

Reactivity of the beta subunit of Escherichia coli adenosine triphosphatase with 4-chloro-7-nitrobenzofurazan.

作者信息

Lunardi J, Satre M, Bof M, Vignais P V

出版信息

Biochemistry. 1979 Nov 27;18(24):5310-6. doi: 10.1021/bi00591a008.

DOI:10.1021/bi00591a008

PMID:42428

Abstract

摘要

相似文献

Reactivity of the beta subunit of Escherichia coli adenosine triphosphatase with 4-chloro-7-nitrobenzofurazan.大肠杆菌三磷酸腺苷酶β亚基与4-氯-7-硝基苯并呋咱的反应活性

Biochemistry. 1979 Nov 27;18(24):5310-6. doi: 10.1021/bi00591a008.

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Non-covalently bound adenine nucleotides in adenosine triphosphatase of Escherichia coli.

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Exploration of adenosine 5'-diphosphate-adenosine 5'-triphosphate binding sites of Escherichia coli adenosine 5'-triphosphatase with arylazido adenine nucleotides.用芳基叠氮腺嘌呤核苷酸对大肠杆菌腺苷5'-三磷酸酶的腺苷5'-二磷酸-腺苷5'-三磷酸结合位点进行探索。

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The mitochondrial ATPase. Selective modification of a nitrogen residue in the beta subunit.

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The interaction of nucleotides with F1-ATPase inactivated with 4-chloro-7-nitrobenzofurazan.

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Catalytic properties of beef heart mitochondrial ATPase modified with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Evidence for catalytic site cooperativity during ATP synthesis.

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The uncA401 mutation alters a nucleotide-binding site in the alpha-subunit of the F1 adenosine triphosphatase from Escherichia coli.uncA401突变改变了来自大肠杆菌的F1三磷酸腺苷酶α亚基中的一个核苷酸结合位点。

FEBS Lett. 1980 Jul 28;116(2):307-9. doi: 10.1016/0014-5793(80)80669-7.

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