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来自大肠杆菌ATP合酶的C亚基的DCCD反应性天冬氨酰残基对F0的构象很重要。

The DCCD-reactive aspartyl-residue of subunit C from the Escherichia coli ATP-synthase is important for the conformation of F0.

作者信息

Friedl P, Hoppe J, Schairer H U

出版信息

Biochem Biophys Res Commun. 1984 Apr 30;120(2):527-33. doi: 10.1016/0006-291x(84)91286-5.

DOI:10.1016/0006-291x(84)91286-5
PMID:6329170
Abstract

The effect of various point mutations in subunits a and and c of the E. coli ATP-synthase was characterized. In each of the mutants there was no F0-dependent H+-conduction, but still an ATPase-activity comparable to wildtype activities. In addition, the subunit b could be extracted from the mutant's F0 but not from the F0 of wildtype. The effects are interpreted as a change in the conformation of F0 caused by the different mutations.

摘要

对大肠杆菌ATP合酶亚基a、b和c中各种点突变的影响进行了表征。在每个突变体中,均不存在F0依赖性H+传导,但仍具有与野生型活性相当的ATP酶活性。此外,亚基b可从突变体的F0中提取出来,但不能从野生型的F0中提取。这些影响被解释为由不同突变导致的F0构象变化。

相似文献

1
The DCCD-reactive aspartyl-residue of subunit C from the Escherichia coli ATP-synthase is important for the conformation of F0.来自大肠杆菌ATP合酶的C亚基的DCCD反应性天冬氨酰残基对F0的构象很重要。
Biochem Biophys Res Commun. 1984 Apr 30;120(2):527-33. doi: 10.1016/0006-291x(84)91286-5.
2
Identification of amino-acid substitutions in the proteolipid subunit of the ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli.从大肠杆菌二环己基碳二亚胺抗性突变体中鉴定ATP合酶蛋白脂质亚基中的氨基酸取代
Eur J Biochem. 1980 Nov;112(1):17-24. doi: 10.1111/j.1432-1033.1980.tb04981.x.
3
Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.来自大肠杆菌的ATP合酶(F1F0)膜部分(F0)的亚基b对于H+转运以及水溶性F1部分的结合是不可或缺的。
Proc Natl Acad Sci U S A. 1984 Dec;81(23):7279-83. doi: 10.1073/pnas.81.23.7279.
4
H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex.二环己基碳二亚胺与F0复合体的单一蛋白脂质(亚基c)反应后,大肠杆菌F1F0的H⁺-ATP酶活性被阻断。
J Biol Chem. 1989 Mar 5;264(7):3896-903.
5
Topological and functional aspects of the proton conductor, F0, of the Escherichia coli ATP-synthase.大肠杆菌ATP合酶质子导体F0的拓扑结构和功能方面
Biosci Rep. 1982 Aug;2(8):631-9. doi: 10.1007/BF01314228.
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Structure and genetics of the H+-conducting F0 portion of the ATP synthase.ATP合酶H⁺传导性F0部分的结构与遗传学
Ann N Y Acad Sci. 1982;402:28-44. doi: 10.1111/j.1749-6632.1982.tb25730.x.
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Directed mutagenesis of the dicyclohexylcarbodiimide-reactive carboxyl residues in beta-subunit of F1-ATPase of Escherichia coli.大肠杆菌F1-ATP酶β亚基中二环己基碳二亚胺反应性羧基残基的定向诱变
Arch Biochem Biophys. 1988 Feb 15;261(1):222-5. doi: 10.1016/0003-9861(88)90121-x.
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Modification of the F0 portion of the H+-translocating adenosinetriphosphatase complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide and effect on the proton channeling function.水溶性碳二亚胺1-乙基-3-[3-(二甲基氨基)丙基]碳二亚胺对大肠杆菌H⁺转运型三磷酸腺苷酶复合物F0部分的修饰及其对质子通道功能的影响。
Biochemistry. 1984 Aug 28;23(18):4128-34. doi: 10.1021/bi00313a018.
9
Chemical modification of F1-ATPase by dicyclohexylcarbodiimide: application to analysis of the stoichiometry of subunits in Escherichia coli F1.二环己基碳二亚胺对F1-ATP酶的化学修饰:应用于大肠杆菌F1中亚基化学计量的分析
Biochemistry. 1982 Sep 14;21(19):4772-6. doi: 10.1021/bi00262a038.
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TFPACD, a novel bifunctional reagent for reacting with DCCD sites in proteins: studies using Escherichia coli ATP synthase.TFPACD,一种用于与蛋白质中DCCD位点反应的新型双功能试剂:使用大肠杆菌ATP合酶的研究
Biochem Biophys Res Commun. 1994 Jun 15;201(2):635-41. doi: 10.1006/bbrc.1994.1748.

引用本文的文献

1
The coupling of the relative movement of the a and c subunits of the F0 to the conformational changes in the F1-ATPase.F0的a亚基和c亚基的相对运动与F1-ATP酶构象变化的偶联。
J Bioenerg Biomembr. 1996 Oct;28(5):415-20. doi: 10.1007/BF02113983.