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1
Rapid type 2 molybdenum(V) electron-paramagnetic resonance signals from xanthine oxidase and the structure of the active centre of the enzyme.来自黄嘌呤氧化酶的快速2型钼(V)电子顺磁共振信号及该酶活性中心的结构
Biochem J. 1980 Mar 1;185(3):767-70. doi: 10.1042/bj1850767.
2
"Rapidly appearing" molybdenum electron-paramagnetic-resonance signals from reduced xanthine oxidase.还原型黄嘌呤氧化酶产生的“快速出现”的钼电子顺磁共振信号。
Biochem J. 1969 Oct;114(4):725-34. doi: 10.1042/bj1140725.
3
The mechanism of action of xanthine oxidase. The relationship between the rapid and very rapid molybdenum electron-paramagnetic-resonance signals.黄嘌呤氧化酶的作用机制。快速和极快速钼电子顺磁共振信号之间的关系。
Biochem J. 1979 Jan 1;177(1):357-60. doi: 10.1042/bj1770357.
4
The molybdenum centre of native xanthine oxidase. Evidence for proton transfer from substrates to the centre and for existence of an anion-binding site.天然黄嘌呤氧化酶的钼中心。质子从底物转移至该中心以及存在阴离子结合位点的证据。
Biochem J. 1978 Dec 1;175(3):869-78. doi: 10.1042/bj1750869.
5
Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum centre of aldehyde oxidase.通过电子顺磁共振光谱法对醛氧化酶钼中心进行的研究。
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6
Coupling of [33S]sulphur to molybdenum(V) in different reduced forms of xanthine oxidase.在不同还原形式的黄嘌呤氧化酶中[33S]硫与钼(V)的偶联
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The nature of the sulphur atom liberated from xanthine oxidase by cyanide. Evidence from e.p.r. spectroscopy after 35S substitution.被氰化物从黄嘌呤氧化酶中释放出的硫原子的性质。35S取代后电子顺磁共振光谱学的证据。
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8
Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase.兔肝醛氧化酶的特性及其与黄嘌呤氧化酶和脱氢酶的关系。
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9
Molybdenum(V) e.p.r. signals obtained from xanthine oxidase on reduction with aldehyde substrates and with 2-amino-4-hydroxy-6-formylpteridine.用醛底物和2-氨基-4-羟基-6-甲酰基蝶啶还原黄嘌呤氧化酶得到的钼(V)电子顺磁共振信号。
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Complex-formation between reduced xanthine oxidase and purine substrates demonstrated by electron paramagnetic resonance.电子顺磁共振证明还原型黄嘌呤氧化酶与嘌呤底物之间的复合物形成。
Biochem J. 1969 Oct;114(4):735-42. doi: 10.1042/bj1140735.

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Xanthine Oxidase-A Personal History.黄嘌呤氧化酶-A 个人史。
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Chem Rev. 2022 Jul 27;122(14):11900-11973. doi: 10.1021/acs.chemrev.1c00914. Epub 2022 Jul 18.
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Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum centre of spinach (Spinacia oleracea) nitrate reductase.通过电子顺磁共振光谱对菠菜(菠菜属)硝酸还原酶的钼中心进行的研究。
Biochem J. 1983 Jul 1;213(1):137-42. doi: 10.1042/bj2130137.
7
Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum centre of aldehyde oxidase.通过电子顺磁共振光谱法对醛氧化酶钼中心进行的研究。
Biochem J. 1982 Apr 1;203(1):263-7. doi: 10.1042/bj2030263.
8
Coupling of [33S]sulphur to molybdenum(V) in different reduced forms of xanthine oxidase.在不同还原形式的黄嘌呤氧化酶中[33S]硫与钼(V)的偶联
Biochem J. 1981 Dec 1;199(3):629-37. doi: 10.1042/bj1990629.
9
Molybdenum(V) e.p.r. signals obtained from xanthine oxidase on reduction with aldehyde substrates and with 2-amino-4-hydroxy-6-formylpteridine.用醛底物和2-氨基-4-羟基-6-甲酰基蝶啶还原黄嘌呤氧化酶得到的钼(V)电子顺磁共振信号。
Biochem J. 1981 Aug 1;197(2):421-5. doi: 10.1042/bj1970421.
10
Oxygen-17 splitting of the very rapid molybdenum(V) e.p.r. signal from xanthine oxidase. Rate of exchange with water of the coupled oxygen atom.来自黄嘌呤氧化酶的极快速钼(V)电子顺磁共振信号的氧-17分裂。与耦合氧原子的水的交换速率。
Biochem J. 1980 Sep 1;189(3):615-23. doi: 10.1042/bj1890615.

本文引用的文献

1
Thiol addition to the carbonyl group. Equilibria and kinetics.硫醇对羰基的加成。平衡与动力学。
J Am Chem Soc. 1966 Sep 5;88(17):3982-94. doi: 10.1021/ja00969a017.
2
The composition of milk xanthine oxidase.牛奶黄嘌呤氧化酶的组成。
Biochem J. 1970 Mar;116(5):851-64. doi: 10.1042/bj1160851.
3
Complex-formation between reduced xanthine oxidase and purine substrates demonstrated by electron paramagnetic resonance.电子顺磁共振证明还原型黄嘌呤氧化酶与嘌呤底物之间的复合物形成。
Biochem J. 1969 Oct;114(4):735-42. doi: 10.1042/bj1140735.
4
"Rapidly appearing" molybdenum electron-paramagnetic-resonance signals from reduced xanthine oxidase.还原型黄嘌呤氧化酶产生的“快速出现”的钼电子顺磁共振信号。
Biochem J. 1969 Oct;114(4):725-34. doi: 10.1042/bj1140725.
5
Electron spin resonance of xanthine oxidase substituted with molybdenum-95.用钼-95取代的黄嘌呤氧化酶的电子自旋共振
Nature. 1966 Oct 29;212(5061):467-9. doi: 10.1038/212467a0.
6
EXAFS studies of the molybdenum center of xanthine oxidase.
J Inorg Biochem. 1979 Oct;11(2):181-6. doi: 10.1016/s0162-0134(00)80182-8.
7
Comparison of the molybdenum centres of native and desulpho xanthine oxidase. The nature of the cyanide-labile sulphur atom and the nature of the proton-accepting group.天然型和脱硫型黄嘌呤氧化酶钼中心的比较。氰化物敏感硫原子的性质和质子接受基团的性质。
Biochem J. 1978 Dec 1;175(3):887-97. doi: 10.1042/bj1750887.
8
The molybdenum centre of native xanthine oxidase. Evidence for proton transfer from substrates to the centre and for existence of an anion-binding site.天然黄嘌呤氧化酶的钼中心。质子从底物转移至该中心以及存在阴离子结合位点的证据。
Biochem J. 1978 Dec 1;175(3):869-78. doi: 10.1042/bj1750869.
9
Electron-paramagnetic-resonance spectroscopy of complexes of xanthine oxidase with xanthine and uric acid.黄嘌呤氧化酶与黄嘌呤和尿酸复合物的电子顺磁共振光谱学
Biochem J. 1978 Jun 1;171(3):653-8. doi: 10.1042/bj1710653.
10
Electron paramagnetic resonance in biochemistry. Computer simulation of spectra from frozen aqueous samples.生物化学中的电子顺磁共振。冷冻水性样品光谱的计算机模拟。
Biochem J. 1978 Jun 1;171(3):649-51. doi: 10.1042/bj1710649.

来自黄嘌呤氧化酶的快速2型钼(V)电子顺磁共振信号及该酶活性中心的结构

Rapid type 2 molybdenum(V) electron-paramagnetic resonance signals from xanthine oxidase and the structure of the active centre of the enzyme.

作者信息

Malthouse J P, Gutteridge S, Bray R C

出版信息

Biochem J. 1980 Mar 1;185(3):767-70. doi: 10.1042/bj1850767.

DOI:10.1042/bj1850767
PMID:6248034
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1161456/
Abstract

Rapid type 2 molybdenum(V) e.p.r. signals from reduced functional xanthine oxidase have been further investigated. These signals, which show strong coupling of two protons to molybdenum, have been obtained under a variety of new conditions: specifically either at pH 8.2 in the presence of borate ions, or at pH 10.1--10.7 with or without various other additions. Parameters of the signals were obtained with the help of computer simulations. In at least some of these signals, the coupled protons must be located on the enzyme rather than on bound species. The relationship between type 1 and type 2 Rapid signals is discussed. They may represent geometrical isomers, or alternatively, hydroxyl uptake as a ligand of molybdenum may be involved in formation of type 2 species.

摘要

对还原型功能性黄嘌呤氧化酶产生的快速2型钼(V)电子顺磁共振信号进行了进一步研究。这些信号显示出两个质子与钼的强耦合,已在多种新条件下获得:具体而言,要么是在pH 8.2且存在硼酸根离子的情况下,要么是在pH 10.1 - 10.7且添加或不添加各种其他物质的情况下。信号参数借助计算机模拟获得。在至少其中一些信号中,耦合质子必定位于酶上而非结合物种上。讨论了1型和2型快速信号之间的关系。它们可能代表几何异构体,或者钼作为配体摄取羟基可能参与了2型物种的形成。