A Novel NADPH:(bound) NADP+ Reductase and NADH:(bound) NADP+ Transhydrogenase Function in Bovine Liver Catalase

Overview

Journal Biochem J

Specialty Biochemistry

Date 2004 Oct 1

PMID 15456401

Citations 12

Authors

Gian F Gaetani

Anna M Ferraris

Paola Sanna

Henry N Kirkman

Affiliations

Soon will be listed here.

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.

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