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Cited by 289

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The function of catalase-bound NADPH.

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Kirkman, H N, Galiano, S, Gaetani, G F·1987·Journal of Biological Chemistry

Abstract

Catalase (H2O2:H2O2 oxidoreductase, EC 1.11.1.6) is of historical interest for having been the subject of some of the earliest investigations of enzymes. A feature of catalase that has been poorly understood for several decades, however, is the mechanism by which catalase remains active in the presence of its own substrate, hydrogen peroxide. We reported recently that catalase contains tightly bound NADPH. The present study with bovine and human catalase revealed that NADPH both prevents and reverses the accumulation of compound II, an inactive form of catalase that is generated slowly when catalase is exposed to hydrogen peroxide. Since the effect of NADPH occurs even at NADPH concentrations below 0.1 microM, the protective mechanism is likely to operate in vivo. This discovery of the role of catalase-bound NADPH brings a unity to the concept of two different mechanisms for disposing of hydrogen peroxide (catalase and the glutathione reductase/peroxidase pathway) by revealing that both mechanisms are dependent on NADPH.

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Metadata

Authors
Kirkman, H. N., Galiano, S., & Gaetani, G. F.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1987-01
Volume
262
Issue
2
Pages
660-666
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1585735064
Cited by
289
References
1
FWCI
3.04
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The function of catalase-bound NADPH. https://app.cochat.ai/papers/10.1016/s0021-9258(19)75835-9
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Kirkman, H. N., Galiano, S., & Gaetani, G. F. (1987). The function of catalase-bound NADPH. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)75835-9

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