Glutathione reductase functions as vanadate(V) reductase

Xianglin Shi; N. S. Dalal

doi:10.1016/0003-9861(90)90262-W

Glutathione reductase functions as vanadate(V) reductase

Xianglin Shi, N. S. Dalal

Toxicology and Cancer Biology

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvment of the superoxide radical. The vanadate(V) reduction was found to be a one-electron transfer process. These results suggest a new pathway for vanadate(V) metabolism and a new function of glutathione reductase.

Original language	English
Pages (from-to)	288-290
Number of pages	3
Journal	Archives of Biochemistry and Biophysics
Volume	278
Issue number	1
DOIs	https://doi.org/10.1016/0003-9861(90)90262-W
State	Published - Apr 1990

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

Access to Document

10.1016/0003-9861(90)90262-W

Cite this

@article{8d43cfac78cd4c7583d6bb1b63292e84,

title = "Glutathione reductase functions as vanadate(V) reductase",

abstract = "The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvment of the superoxide radical. The vanadate(V) reduction was found to be a one-electron transfer process. These results suggest a new pathway for vanadate(V) metabolism and a new function of glutathione reductase.",

author = "Xianglin Shi and Dalal, {N. S.}",

year = "1990",

month = apr,

doi = "10.1016/0003-9861(90)90262-W",

language = "English",

volume = "278",

pages = "288--290",

number = "1",

}

TY - JOUR

T1 - Glutathione reductase functions as vanadate(V) reductase

AU - Shi, Xianglin

AU - Dalal, N. S.

PY - 1990/4

Y1 - 1990/4

N2 - The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvment of the superoxide radical. The vanadate(V) reduction was found to be a one-electron transfer process. These results suggest a new pathway for vanadate(V) metabolism and a new function of glutathione reductase.

AB - The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvment of the superoxide radical. The vanadate(V) reduction was found to be a one-electron transfer process. These results suggest a new pathway for vanadate(V) metabolism and a new function of glutathione reductase.

UR - http://www.scopus.com/inward/record.url?scp=0025366163&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025366163&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(90)90262-W

DO - 10.1016/0003-9861(90)90262-W

M3 - Article

C2 - 2157361

AN - SCOPUS:0025366163

SN - 0003-9861

VL - 278

SP - 288

EP - 290

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 1

ER -

Glutathione reductase functions as vanadate(V) reductase

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this