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Studies on nicotinamide adenine dinucleotide phosphate reductase of spinach chloroplasts.

作者信息

Keirns J J, Wang J H

出版信息

J Biol Chem. 1972 Nov 25;247(22):7374-82.

PMID:4404748
Abstract
摘要

相似文献

1
Studies on nicotinamide adenine dinucleotide phosphate reductase of spinach chloroplasts.
J Biol Chem. 1972 Nov 25;247(22):7374-82.
2
Kinetics of extraction of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase from spinach chloroplasts.
Arch Biochem Biophys. 1982 Jan;213(1):67-72. doi: 10.1016/0003-9861(82)90440-4.
3
On the structure and function of reduced nicotinamide adenine dinucleotide phosphate-cytochrome f reductase of spinach chloroplasts.菠菜叶绿体中还原型烟酰胺腺嘌呤二核苷酸磷酸 - 细胞色素f还原酶的结构与功能
Eur J Biochem. 1968 Feb;3(4):461-72. doi: 10.1111/j.1432-1033.1967.tb19553.x.
4
Partial separation and interconversion of NADH- and NADPH-linked activities of purified glyceraldehyde 3-phosphate dehydrogenase from spinach chloroplasts.菠菜叶绿体中纯化的3-磷酸甘油醛脱氢酶的NADH和NADPH相关活性的部分分离与相互转化
FEBS Lett. 1974 Jun 15;42(3):285-8. doi: 10.1016/0014-5793(74)80747-7.
5
Studies on adrenal steroid hydroxylases. Molecular and catalytic properties of adrenodoxin reductase (a flavoprotein).肾上腺类固醇羟化酶的研究。肾上腺铁氧化还原蛋白还原酶（一种黄素蛋白）的分子和催化特性。
J Biol Chem. 1973 Mar 25;248(6):2089-94.
6
Identification and structure of a novel flavin prosthetic group associated with reduced nicotinamide adenine dinucleotide dehydrogenase from Peptostreptococcus elsdenii.与埃尔氏消化链球菌中烟酰胺腺嘌呤二核苷酸脱氢酶相关的一种新型黄素辅基的鉴定与结构
J Biol Chem. 1973 Sep 25;248(18):6568-70.
7
Some properties of hepatic reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase.肝脏还原型烟酰胺腺嘌呤二核苷酸磷酸 - 细胞色素c还原酶的一些特性
Biochemistry. 1973 Jun 5;12(12):2297-308. doi: 10.1021/bi00736a018.
8
On the reactivity of the sulfhydryl groups of ferredoxin nicotinamide adenine dinucleotide phosphate reductase.关于铁氧化还原蛋白烟酰胺腺嘌呤二核苷酸磷酸还原酶巯基的反应活性
J Biol Chem. 1969 Sep 10;244(17):4757-60.
9
The structural properties of spinach leaf glyoxylic acid reductase.菠菜叶乙醛酸还原酶的结构特性
J Biol Chem. 1970 Aug 10;245(15):3821-30.
10
Purification and characterization of yeast thioredoxin reductase.酵母硫氧还蛋白还原酶的纯化与特性分析
Biochim Biophys Acta. 1973 Dec 19;327(2):274-81. doi: 10.1016/0005-2744(73)90410-5.

引用本文的文献

1
Light-Independent Nitrogen Assimilation in Plant Leaves: Nitrate Incorporation into Glutamine, Glutamate, Aspartate, and Asparagine Traced by N.植物叶片中的光独立氮同化：通过氮追踪硝酸盐掺入谷氨酰胺、谷氨酸、天冬氨酸和天冬酰胺的过程
Plants (Basel). 2020 Oct 2;9(10):1303. doi: 10.3390/plants9101303.
2
On the Natural History of Flavin-Based Electron Bifurcation.基于黄素的电子分叉的自然史
Front Microbiol. 2018 Jul 3;9:1357. doi: 10.3389/fmicb.2018.01357. eCollection 2018.
3
Ferredoxin-NADP(+) reductase, a nuclearly-coded enzyme unaffected by tentoxin treatment.
铁氧还蛋白-NADP(+)还原酶，一种核编码的酶，不受 tentoxin 处理的影响。
Photosynth Res. 1985 Jan;6(2):113-20. doi: 10.1007/BF00032786.
4
Effect of Ferredoxin on the Diaphorase Activity of Cyanobacterial Ferredoxin-NADP Reductase.铁氧还蛋白对蓝细菌铁氧还蛋白-NADP 还原酶的黄递酶活性的影响。
Plant Physiol. 1985 Jan;77(1):229-31. doi: 10.1104/pp.77.1.229.
5
How is Ferredoxin-NADP Reductase Involved in the NADP Photoreduction of Chloroplasts?铁氧还蛋白-NADP还原酶如何参与叶绿体的NADP光还原？
Photosynth Res. 2004;80(1-3):307-13. doi: 10.1023/B:PRES.0000030456.96329.f9.
6
Electron donation to the flavoprotein NifL, a redox-sensing transcriptional regulator.向黄素蛋白NifL（一种氧化还原感应转录调节因子）提供电子。
Biochem J. 1998 Jun 1;332 ( Pt 2)(Pt 2):413-9. doi: 10.1042/bj3320413.
7
Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin.黄素蛋白还原酶扩展家族的结构原型：邻苯二甲酸双加氧酶还原酶与铁氧化还原蛋白还原酶及铁氧化还原蛋白的比较
Protein Sci. 1993 Dec;2(12):2112-33. doi: 10.1002/pro.5560021212.
8
Structure-function relations for ferredoxin reductase.铁氧化还原蛋白还原酶的结构-功能关系
J Bioenerg Biomembr. 1994 Feb;26(1):89-99. doi: 10.1007/BF00763221.
9
Correlation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron transfer proteins.还原速率常数与氧化还原电位之间的相关性作为电子传递蛋白反应机制系统研究的基础。
Proc Natl Acad Sci U S A. 1983 Nov;80(22):6740-4. doi: 10.1073/pnas.80.22.6740.