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1H, 13C, 15N backbone and sidechain resonance assignments of apo-NosL, a novel copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes.

作者信息

Taubner Lara M, McGuirl Michele A, Dooley David M, Copié Valérie

出版信息

J Biomol NMR. 2004 Jun;29(2):211-2. doi: 10.1023/B:JNMR.0000019240.29152.ac.

DOI:10.1023/B:JNMR.0000019240.29152.ac
PMID:15014237
Abstract
摘要

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本文引用的文献

1
Requirements for Cu(A) and Cu-S center assembly of nitrous oxide reductase deduced from complete periplasmic enzyme maturation in the nondenitrifier Pseudomonas putida.从非反硝化菌恶臭假单胞菌周质酶完全成熟过程推断一氧化二氮还原酶铜（A）和铜硫中心组装的要求
J Bacteriol. 2003 Feb;185(3):887-96. doi: 10.1128/JB.185.3.887-896.2003.
2
Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster.一氧化二氮还原酶（nos）基因簇的新型铜（I）蛋白NosL的表达、纯化及特性分析
J Biol Inorg Chem. 2001 Feb;6(2):189-95. doi: 10.1007/s007750000190.
3
Structure and chemistry of the copper chaperone proteins.
铜伴侣蛋白的结构与化学性质。
Curr Opin Chem Biol. 2000 Apr;4(2):140-7. doi: 10.1016/s1367-5931(99)00066-6.
4
The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: cloning, sequence analysis, and expression.来自土壤细菌解环无色杆菌的一氧化二氮还原酶（nos）基因簇：克隆、序列分析及表达
J Inorg Biochem. 1998 Jul;70(3-4):155-69. doi: 10.1016/s0162-0134(98)10001-6.
5
Mutation of the conserved Cys165 outside of the CuA domain destabilizes nitrous oxide reductase but maintains its catalytic activity. Evidence for disulfide bridges and a putative protein disulfide isomerase gene.铜A结构域外保守的半胱氨酸165发生突变会使一氧化二氮还原酶不稳定，但能维持其催化活性。二硫键和一个假定的蛋白质二硫键异构酶基因的证据。
Eur J Biochem. 1996 Apr 15;237(2):447-53. doi: 10.1111/j.1432-1033.1996.0447k.x.
6
Nitrous oxide reductase from denitrifying Pseudomonas stutzeri. Genes for copper-processing and properties of the deduced products, including a new member of the family of ATP/GTP-binding proteins.反硝化施氏假单胞菌的一氧化二氮还原酶。铜加工相关基因及推导产物的特性，包括ATP/GTP结合蛋白家族的一个新成员。
Eur J Biochem. 1990 Sep 24;192(3):591-9. doi: 10.1111/j.1432-1033.1990.tb19265.x.