The Redox Properties of a Cysteine Tryptophylquinone-Dependent Glycine Oxidase Are Distinct from Those of Tryptophylquinone-Dependent Dehydrogenases.

The Redox Properties of a Cysteine Tryptophylquinone-Dependent Glycine Oxidase Are Distinct from Those of Tryptophylquinone-Dependent Dehydrogenases.
复制标题

半胱氨酸色氨醌依赖性甘氨酸氧化酶的氧化还原性质与色氨醌依赖性脱氢酶的氧化还原性质不同。

DOI:
10.1021/acs.biochem.9b00104
复制
发表时间:
2019
期刊:
影响因子:
2.9
通讯作者:
Davidson,VictorL
Davidson,VictorL
中科院分区:
生物学3区
文献类型:
--
作者:
Ma,Zhongxin;Davidson,VictorL

文献摘要

参考文献

相似文献

GoxA是一种依赖于半胱氨酸色氨酸醌(CTQ)的甘氨酸氧化酶,是loda样蛋白家族的成员。测定了醌/半醌偶和半醌/喹啉偶的电化学中点电位(Em)分别为111和21。整体双电子醌/醌对的emvalue与CTQ-和色氨酸-色氨酸醌(TTQ)脱氢酶的emvalue相似。然而,对于ttq依赖的甲胺脱氢酶,醌/半醌对比半醌/喹啉对更负,与GoxA相反。GoxA中CTQ的双电子醌/醌偶emvalue随pH的变化表明整个双电子转移过程与一个质子的转移有关。因此,喹啉是阴离子的。本文报道的数据进一步表明,在GoxA中,CTQ半醌是中性的,与TTQ依赖的脱氢酶相反,它是阴离子TTQ半醌。这些结果是在结构和功能的背景下讨论这种甘氨酸氧化酶,比较色氨酸依赖脱氢酶。
GoxA is a cysteine tryptophylquinone (CTQ)-dependent glycine oxidase that is a member of a family of LodA-like proteins. The electrochemical midpoint potential (Em) values for the quinone/semiquinone couple and the semiquinone/quinol couple were determined to be 111 and 21, respectively. TheEmvalue for the overall two-electron quinone/quinol couple was similar to those of CTQ- and tryptophan tryptophylquinone (TTQ)-bearing dehydrogenases. However, for the well-studied TTQ-dependent methylamine dehydrogenase, the quinone/semiquinone couple is more negative than the semiquinone/quinol couple, the opposite of what was determined for GoxA. The change inEmvalue for the two-electron quinone/quinol couple of CTQ in GoxA with pH indicates that the overall two-electron transfer process is associated with the transfer of one proton. Thus, the quinol is anionic. The data reported herein further suggest that in GoxA the CTQ semiquinone is neutral, in contrast to the TTQ-dependent dehydrogenases, in which it is an anionic TTQ semiquinone. These results are discussed in the context of the structure and function of this glycine oxidase, compared to that of the tryptophylquinone-dependent dehydrogenases.
GoxA 与其修饰酶及其亚基组装的相互作用取决于半胱氨酸色氨酸醌生物合成的程度。
DOI: 10.1021/acs.biochem.6b00274
发表时间: 2016
期刊: Biochemistry
影响因子: 2.9
作者:
Sehanobish,Esha;Campillo-Brocal,JonatanC;Williamson,HeatherR;Sanchez-Amat,Antonio;Davidson,VictorL
通讯作者: Davidson,VictorL
DOI: 10.1046/j.1432-1033.2003.03474.x
发表时间: 2003-03-01
期刊: EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子: --
作者:
Finn, RD;Basran, J;Scrutton, NS
通讯作者: Scrutton, NS
DOI: 10.1021/acs.biochem.8b00123
发表时间: 2018-06-05
期刊: Biochemistry
影响因子: 2.9
作者:
Davidson VL
通讯作者: Davidson VL
DOI: 10.1021/bi035062r
发表时间: 2003-09
期刊: Biochemistry
影响因子: 2.9
作者:
Dapeng Sun;K. Ono;T. Okajima;K. Tanizawa;M. Uchida;Yukio Yamamoto*;F. Mathews;V. Davidson
通讯作者: Dapeng Sun;K. Ono;T. Okajima;K. Tanizawa;M. Uchida;Yukio Yamamoto*;F. Mathews;V. Davidson
DOI: 10.1021/cr400475g
发表时间: 2014-04-23
期刊: CHEMICAL REVIEWS
影响因子: 62.1
作者:
Klinman, Judith P.;Bonnot, Florence
通讯作者: Bonnot, Florence