异常汉逊酵母黄素细胞色素b2（黄素脱氢酶和b2核心）的黄素和血红素结构域在大肠杆菌中的表达及重组蛋白的表征
Expression in Escherichia coli of the flavin and the haem domains of Hansenula anomala flavocytochrome b2 (flavodehydrogenase and b2 core) and characterization of the recombinant proteins.
作者信息
Silvestrini M C, Tegoni M, Célerier J, Desbois A, Gervais M
机构信息
Dipartimento di Scienze Biochimiche, Università di Roma La Sapienza, Italy.
出版信息
Biochem J. 1993 Oct 15;295 ( Pt 2)(Pt 2):501-8. doi: 10.1042/bj2950501.
Abstract
The flavin and haem domains of Hansenula anomala flavocytochrome b2 have been independently expressed in Escherichia coli. The flavin domain activity, studied only in the total cellular extract, owing to its instability, has characteristics very similar to those of the flavin domain obtained by proteolysis. The haem domain (r-core) has been purified to homogeneity and characterized in detail from spectroscopic and functional points of view. Spectral differences with respect to the domain produced by proteolysis (p-core) were found using resonance Raman and c.d. spectroscopy and have been interpreted in terms of changes in haem-protein interactions. However, this structural difference is functionally silent, since the r-core is able to reduce cytochrome c with the same efficiency as the proteolytic domain.
摘要
异常汉逊酵母黄素细胞色素b2的黄素结构域和血红素结构域已在大肠杆菌中独立表达。由于黄素结构域不稳定，仅在全细胞提取物中研究了其活性，其特性与通过蛋白水解获得的黄素结构域非常相似。血红素结构域（r-核心）已纯化至同质，并从光谱学和功能角度进行了详细表征。使用共振拉曼光谱和圆二色光谱发现了与蛋白水解产生的结构域（p-核心）相比的光谱差异，并根据血红素-蛋白质相互作用的变化进行了解释。然而，这种结构差异在功能上是沉默的，因为r-核心能够以与蛋白水解结构域相同的效率还原细胞色素c。
相似文献
1
Expression in Escherichia coli of the flavin and the haem domains of Hansenula anomala flavocytochrome b2 (flavodehydrogenase and b2 core) and characterization of the recombinant proteins.异常汉逊酵母黄素细胞色素b2（黄素脱氢酶和b2核心）的黄素和血红素结构域在大肠杆菌中的表达及重组蛋白的表征
Biochem J. 1993 Oct 15;295 ( Pt 2)(Pt 2):501-8. doi: 10.1042/bj2950501.
2
Proteolytic cleavage of Hansenula anomala flavocytochrome b2 into its two functional domains. Isolation of a highly active flavodehydrogenase and a cytochrome b2 core.异常汉逊酵母黄素细胞色素b2蛋白水解裂解为其两个功能结构域。高活性黄素脱氢酶和细胞色素b2核心的分离。
Eur J Biochem. 1983 Feb 1;130(2):253-9. doi: 10.1111/j.1432-1033.1983.tb07144.x.
3
Isolation and characterization of the flavin-binding domain of flavocytochrome b2 expressed independently in Escherichia coli.在大肠杆菌中独立表达的黄素细胞色素b2黄素结合结构域的分离与鉴定。
Biochem J. 1995 Jul 15;309 ( Pt 2)(Pt 2):601-5. doi: 10.1042/bj3090601.
4
Isolation of the flavodehydrogenase domain of Hansenula anomala flavocytochrome b2 after mild proteolysis by an H. anomala proteinase.异常汉逊酵母蛋白酶轻度蛋白酶解后分离异常汉逊酵母黄素细胞色素b2的黄素脱氢酶结构域。
Eur J Biochem. 1989 Jun 1;182(1):67-75. doi: 10.1111/j.1432-1033.1989.tb14801.x.
5
Interaction between cytochrome b2 core and flavodehydrogenase from the yeast Hansenula anomala.
Photochem Photobiol. 1997 Jul;66(1):72-5. doi: 10.1111/j.1751-1097.1997.tb03140.x.
6
Electron-transfer steps involved in the reactivity of Hansenula anomala flavocytochrome b2 as deduced from deuterium isotope effects and simulation studies.从氘同位素效应和模拟研究推断异常汉逊酵母黄素细胞色素b2反应性中涉及的电子转移步骤。
Biochem J. 1991 Feb 15;274 ( Pt 1)(Pt 1):207-17. doi: 10.1042/bj2740207.
7
L-Mandelate dehydrogenase from Rhodotorula graminis: cloning, sequencing and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain.来自禾本科红酵母的L-扁桃酸脱氢酶：重组酶及其独立表达的黄素结构域的克隆、测序和动力学表征
Biochem J. 1998 Jul 1;333 ( Pt 1)(Pt 1):107-15. doi: 10.1042/bj3330107.
8
Probing intramolecular electron transfer within flavocytochrome b2 with a monoclonal antibody.利用单克隆抗体探究黄素细胞色素b2分子内的电子转移
Biochemistry. 1998 Mar 10;37(10):3440-8. doi: 10.1021/bi972639u.
9
The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b2.黄素细胞色素b2中分子内电子转移过程中结构域间铰链的重要性。
Biochem J. 1993 Apr 1;291 ( Pt 1)(Pt 1):89-94. doi: 10.1042/bj2910089.
10
Nucleotide sequence of the Hansenula anomala gene encoding flavocytochrome b2 (L-lactate:cytochrome c oxidoreductase).异常汉逊酵母中编码黄素细胞色素b2（L-乳酸：细胞色素c氧化还原酶）的基因的核苷酸序列。
Nucleic Acids Res. 1989 Oct 25;17(20):8381. doi: 10.1093/nar/17.20.8381.
引用本文的文献
1
Flavocytochrome -Mediated Electroactive Nanoparticles for Developing Amperometric L-Lactate Biosensors.基于 flavocytochrome 的电活性纳米颗粒用于开发安培型 L-乳酸生物传感器。
Biosensors (Basel). 2023 May 28;13(6):587. doi: 10.3390/bios13060587.
本文引用的文献
1
Spectrum of horse-heart cytochrome c.马心细胞色素c的光谱
Biochem J. 1959 Mar;71(3):570-2. doi: 10.1042/bj0710570.
2
Potentiometric and other studies on preparations of cytochrome c from ox- and horse-heart muscle.关于从牛心和马心肌中制备细胞色素c的电位测定及其他研究。
Biochem J. 1956 Jan;62(1):21-9. doi: 10.1042/bj0620021.
3
A flavin-mononucleotide-binding site in Hansenula anomala nicked flavocytochrome b2, requiring the association of two domains.异常汉逊酵母切口黄素细胞色素b2中的黄素单核苷酸结合位点，需要两个结构域的缔合。
Eur J Biochem. 1980 Oct;111(1):17-31. doi: 10.1111/j.1432-1033.1980.tb06071.x.
4
Proton nuclear nagnetic resonance characterization of heme disorder in monomeric insect hemoglobins.单体昆虫血红蛋白中血红素紊乱的质子核磁共振表征
J Biol Chem. 1980 Jan 10;255(1):66-70.
5
Imported mitochondrial proteins cytochrome b2 and cytochrome c1 are processed in two steps.导入的线粒体蛋白细胞色素b2和细胞色素c1分两步进行加工。
Proc Natl Acad Sci U S A. 1982 Jan;79(2):267-71. doi: 10.1073/pnas.79.2.267.
6
Spontaneous dissociation of a cytochrome core and a biglobular flavoprotein after mild trypsinolysis of the bifunctional Saccharomyces cerevisiae flavocytochrome b2.对双功能酿酒酵母黄素细胞色素b2进行温和胰蛋白酶消化后，细胞色素核心与大球状黄素蛋白的自发解离
Eur J Biochem. 1980 Oct;111(2):357-67. doi: 10.1111/j.1432-1033.1980.tb04949.x.
7
Proteolytic cleavage of Hansenula anomala flavocytochrome b2 into its two functional domains. Isolation of a highly active flavodehydrogenase and a cytochrome b2 core.异常汉逊酵母黄素细胞色素b2蛋白水解裂解为其两个功能结构域。高活性黄素脱氢酶和细胞色素b2核心的分离。
Eur J Biochem. 1983 Feb 1;130(2):253-9. doi: 10.1111/j.1432-1033.1983.tb07144.x.
8
Transient kinetics of the one-electron transfer reaction between reduced flavocytochrome b2 and oxidized cytochrome c. Evidence for the existence of a protein complex in the reaction.还原型黄素细胞色素b2与氧化型细胞色素c之间单电子转移反应的瞬态动力学。反应中存在蛋白质复合物的证据。
Eur J Biochem. 1982 Nov 15;128(2-3):533-42. doi: 10.1111/j.1432-1033.1982.tb06998.x.
9
[Study by circular dichroism of the heme-flavin-protein interactions of the cytochrome b2 (L-lactate oxoreductase) of the liver].[肝脏细胞色素b2（L-乳酸氧化还原酶）血红素-黄素-蛋白质相互作用的圆二色性研究]
Eur J Biochem. 1969 Jun;9(2):280-5. doi: 10.1111/j.1432-1033.1969.tb00606.x.
10
Molecular weight and quaternary structure of yeast L-lactate dehydrogenase (cytochrome b2). 2. Revised heme extinction coefficients and minimal molecular weight.酵母L-乳酸脱氢酶（细胞色素b2）的分子量和四级结构。2. 修正后的血红素消光系数和最小分子量。
Eur J Biochem. 1970 Jan;12(1):158-64. doi: 10.1111/j.1432-1033.1970.tb00833.x.
Zotero 插件