质子转运还原型泛醌在大肠杆菌呼吸链硝酸还原酶区段的跨膜定位。 - Suppr

Suppr

超能文献

A transmembrane location for the proton-translocating reduced ubiquinone leads to nitrate reductase segment of the respiration chain of Escherichia coli.

作者信息

Boxer D H, Clegg R A

出版信息

FEBS Lett. 1975 Dec 1;60(1):54-7. doi: 10.1016/0014-5793(75)80417-0.

DOI:10.1016/0014-5793(75)80417-0

PMID:58794

Abstract

摘要

相似文献

A transmembrane location for the proton-translocating reduced ubiquinone leads to nitrate reductase segment of the respiration chain of Escherichia coli.质子转运还原型泛醌在大肠杆菌呼吸链硝酸还原酶区段的跨膜定位。

FEBS Lett. 1975 Dec 1;60(1):54-7. doi: 10.1016/0014-5793(75)80417-0.

NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing.大肠杆菌K-12周质硝酸还原酶的NapGH组件：在喹啉氧化和氧化还原平衡中的定位、拓扑结构及生理作用

Biochem J. 2004 Apr 1;379(Pt 1):47-55. doi: 10.1042/BJ20031115.

The mechanism of proton translocation driven by the respiratory nitrate reductase complex of Escherichia coli.大肠杆菌呼吸硝酸盐还原酶复合物驱动质子转运的机制。

Biochem J. 1980 Jul 15;190(1):79-94. doi: 10.1042/bj1900079.

Proton translocation and the respiratory nitrate reductase of Escherichia coli.质子转运与大肠杆菌的呼吸型硝酸还原酶

Biochem J. 1975 Dec;152(3):547-59. doi: 10.1042/bj1520547.

Topography of nitrate reductase of the cytoplasmic membrane of Escherichia coli: the nitrate-reducing site [proceedings].大肠杆菌细胞质膜硝酸还原酶的拓扑结构：硝酸还原位点[会议论文集]

Biochem Soc Trans. 1978;6(6):1287-9. doi: 10.1042/bst0061287.

Substrate binding site for nitrate reductase of Escherichia coli is on the inner aspect of the membrane.大肠杆菌硝酸还原酶的底物结合位点位于膜的内侧。

J Bacteriol. 1979 Mar;137(3):1227-33. doi: 10.1128/jb.137.3.1227-1233.1979.

The proton-consuming site of the respiratory nitrate reductase of Escherichia coli is on the cytoplasmic aspect of the cytoplasmic membrane [proceedings].大肠杆菌呼吸型硝酸还原酶的质子消耗位点位于细胞质膜的细胞质一侧[会议论文集]。

Biochem Soc Trans. 1978;6(2):416-8. doi: 10.1042/bst0060416.

Arrangement of respiratory nitrate reductase in the cytoplasmic membrane of Escherichia coli. Location of beta subunit.呼吸型硝酸还原酶在大肠杆菌细胞质膜中的排列。β亚基的定位。

FEBS Lett. 1980 Apr 21;113(1):15-20. doi: 10.1016/0014-5793(80)80484-4.

Aerobic and anaerobic bacterial respiration monitored by electrodes.通过电极监测需氧和厌氧细菌呼吸。

J Gen Microbiol. 1977 Jan;98(1):231-8. doi: 10.1099/00221287-98-1-231.

Solubilization of Escherichia coli nitrate reductase by a membrane-bound protease.膜结合蛋白酶对大肠杆菌硝酸还原酶的增溶作用。

J Bacteriol. 1975 Mar;121(3):1102-10. doi: 10.1128/jb.121.3.1102-1110.1975.

引用本文的文献

The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli.甲酸脱氢酶在大肠杆菌细胞质膜中的组织形式。

Biochem J. 1981 Jun 1;195(3):627-37. doi: 10.1042/bj1950627.

The respiratory chains of Escherichia coli.大肠杆菌的呼吸链

Microbiol Rev. 1984 Sep;48(3):222-71. doi: 10.1128/mr.48.3.222-271.1984.

The mechanism of proton translocation driven by the respiratory nitrate reductase complex of Escherichia coli.大肠杆菌呼吸硝酸盐还原酶复合物驱动质子转运的机制。

Biochem J. 1980 Jul 15;190(1):79-94. doi: 10.1042/bj1900079.

Identification and localization of enzymes of the fumarate reductase and nitrate respiration systems of escherichia coli by crossed immunoelectrophoresis.通过交叉免疫电泳法对大肠杆菌延胡索酸还原酶和硝酸盐呼吸系统的酶进行鉴定和定位。

J Bacteriol. 1983 Feb;153(2):1027-37. doi: 10.1128/jb.153.2.1027-1037.1983.

Nitrate respiration in relation to facultative metabolism in enterobacteria.肠杆菌中与兼性代谢相关的硝酸盐呼吸作用

Microbiol Rev. 1988 Jun;52(2):190-232. doi: 10.1128/mr.52.2.190-232.1988.

Energy conservation in chemotrophic anaerobic bacteria.化能营养型厌氧细菌中的能量守恒

Bacteriol Rev. 1977 Mar;41(1):100-80. doi: 10.1128/br.41.1.100-180.1977.

Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Effects of permeability barriers imposed by the cytoplasmic membrane.联吡啶鎓化合物与大肠杆菌厌氧呼吸酶反应的位点及特异性。细胞质膜形成的通透性屏障的影响。

Biochem J. 1977 Apr 15;164(1):199-211. doi: 10.1042/bj1640199.

Bacterial respiration.细菌呼吸作用

Bacteriol Rev. 1977 Mar;41(1):47-99. doi: 10.1128/br.41.1.47-99.1977.

文献AI研究员

20分钟写一篇综述，助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型，支持多种主流文档格式。

立即体验