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Biochem J. 2005 Feb 1;385(Pt 3):763-8.

A novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase.

Author information

1
Division of Hematological Oncology, Istituto Nazionale per la Ricerca sul Cancro and Dipartimento di Medicina Interna, University of Genoa, 16132 Genoa, Italy.

Abstract

Many catalases have the shared property of containing bound NADPH and being susceptible to inactivation by their own substrate, H2O2. The presence of additional (unbound) NADPH effectively prevents bovine liver and human erythrocytic catalase from becoming compound II, the reversibly inactivated state of catalase, and NADP+ is known to be generated in the process. The function of the bound NADPH, which is tightly bound in bovine liver catalase, has been unknown. The present study with bovine liver catalase and [14C]NADPH and [14C]NADH revealed that unbound NADPH or NADH are substrates for an internal reductase and transhydrogenase reaction respectively; the unbound NADPH or NADH cause tightly bound NADP+ to become NADPH without becoming tightly bound themselves. This and other results provide insight into the function of tightly bound NADPH.

PMID:
15456401
PMCID:
PMC1134752
DOI:
10.1042/BJ20041495
[Indexed for MEDLINE]
Free PMC Article

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