Superoxide reactivates nitric oxide-inhibited catalase

Yu Shin Kim, S. Han

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Catalase binds nitric oxide (NO) to generate ferricatalase-NO, an inhibited form of the enzyme. Superoxide (O2 -) is also an inactivator of the enzyme. We found, however, that O2 - efficiently converted the inhibited ferricatalase-NO to the active ferricatalase without producing detectable intermediates. The reaction slowed down when O2 - was disproportionated to H2O2 and O2 by superoxide dismutase, but H2O2 could displace the heme-bound NO slowly to regenerate ferricatalase. Reactivation was observed even under simultaneous generation of NO and O2 -, suggesting that ferricatalase-NO reacts with O2 - fast enough to compete with the rapid reaction of O2 - and NO. Formation of peroxynitrite by the simultaneous generation of NO and O2 - was only partially inhibited by ferricatalase, presumably due to slow binding of NO to catalase in comparison with the reaction of NO and O2 -.

Original languageEnglish (US)
Pages (from-to)1269-1271
Number of pages3
JournalBiological Chemistry
Volume381
Issue number12
DOIs
StatePublished - 2000
Externally publishedYes

Fingerprint

Superoxides
Catalase
Nitric Oxide
Peroxynitrous Acid
Enzymes
Heme
Superoxide Dismutase

Keywords

  • Catalase
  • Nitric oxide
  • Superoxide

ASJC Scopus subject areas

  • Biochemistry

Cite this

Superoxide reactivates nitric oxide-inhibited catalase. / Kim, Yu Shin; Han, S.

In: Biological Chemistry, Vol. 381, No. 12, 2000, p. 1269-1271.

Research output: Contribution to journalArticle

Kim, Yu Shin ; Han, S. / Superoxide reactivates nitric oxide-inhibited catalase. In: Biological Chemistry. 2000 ; Vol. 381, No. 12. pp. 1269-1271.
@article{7fa3dab14b50490fb315c4bf8406f99f,
title = "Superoxide reactivates nitric oxide-inhibited catalase",
abstract = "Catalase binds nitric oxide (NO) to generate ferricatalase-NO, an inhibited form of the enzyme. Superoxide (O2 -) is also an inactivator of the enzyme. We found, however, that O2 - efficiently converted the inhibited ferricatalase-NO to the active ferricatalase without producing detectable intermediates. The reaction slowed down when O2 - was disproportionated to H2O2 and O2 by superoxide dismutase, but H2O2 could displace the heme-bound NO slowly to regenerate ferricatalase. Reactivation was observed even under simultaneous generation of NO and O2 -, suggesting that ferricatalase-NO reacts with O2 - fast enough to compete with the rapid reaction of O2 - and NO. Formation of peroxynitrite by the simultaneous generation of NO and O2 - was only partially inhibited by ferricatalase, presumably due to slow binding of NO to catalase in comparison with the reaction of NO and O2 -.",
keywords = "Catalase, Nitric oxide, Superoxide",
author = "Kim, {Yu Shin} and S. Han",
year = "2000",
doi = "10.1515/BC.2000.156",
language = "English (US)",
volume = "381",
pages = "1269--1271",
journal = "Biological Chemistry",
issn = "1431-6730",
publisher = "Walter de Gruyter GmbH & Co. KG",
number = "12",

}

TY - JOUR

T1 - Superoxide reactivates nitric oxide-inhibited catalase

AU - Kim, Yu Shin

AU - Han, S.

PY - 2000

Y1 - 2000

N2 - Catalase binds nitric oxide (NO) to generate ferricatalase-NO, an inhibited form of the enzyme. Superoxide (O2 -) is also an inactivator of the enzyme. We found, however, that O2 - efficiently converted the inhibited ferricatalase-NO to the active ferricatalase without producing detectable intermediates. The reaction slowed down when O2 - was disproportionated to H2O2 and O2 by superoxide dismutase, but H2O2 could displace the heme-bound NO slowly to regenerate ferricatalase. Reactivation was observed even under simultaneous generation of NO and O2 -, suggesting that ferricatalase-NO reacts with O2 - fast enough to compete with the rapid reaction of O2 - and NO. Formation of peroxynitrite by the simultaneous generation of NO and O2 - was only partially inhibited by ferricatalase, presumably due to slow binding of NO to catalase in comparison with the reaction of NO and O2 -.

AB - Catalase binds nitric oxide (NO) to generate ferricatalase-NO, an inhibited form of the enzyme. Superoxide (O2 -) is also an inactivator of the enzyme. We found, however, that O2 - efficiently converted the inhibited ferricatalase-NO to the active ferricatalase without producing detectable intermediates. The reaction slowed down when O2 - was disproportionated to H2O2 and O2 by superoxide dismutase, but H2O2 could displace the heme-bound NO slowly to regenerate ferricatalase. Reactivation was observed even under simultaneous generation of NO and O2 -, suggesting that ferricatalase-NO reacts with O2 - fast enough to compete with the rapid reaction of O2 - and NO. Formation of peroxynitrite by the simultaneous generation of NO and O2 - was only partially inhibited by ferricatalase, presumably due to slow binding of NO to catalase in comparison with the reaction of NO and O2 -.

KW - Catalase

KW - Nitric oxide

KW - Superoxide

UR - http://www.scopus.com/inward/record.url?scp=0034513773&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034513773&partnerID=8YFLogxK

U2 - 10.1515/BC.2000.156

DO - 10.1515/BC.2000.156

M3 - Article

VL - 381

SP - 1269

EP - 1271

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

IS - 12

ER -