[HTML][HTML] Mechanisms of protection of catalase by NADPH: kinetics and stoichiometry
HN Kirkman, M Rolfo, AM Ferraris… - Journal of Biological …, 1999 - ASBMB
NADPH is known to be tightly bound to mammalian catalase and to offset the ability of the
substrate of catalase (H 2 O 2) to convert the enzyme to an inactive state (compound II). In
the process, the bound NADPH becomes NADP+ and is replaced by another molecule of
NADPH. This protection is believed to occur through electron tunneling between NADPH on
the surface of the catalase and the heme group within the enzyme. The present study
provided additional support for the concept of an intermediate state of catalase, through …
substrate of catalase (H 2 O 2) to convert the enzyme to an inactive state (compound II). In
the process, the bound NADPH becomes NADP+ and is replaced by another molecule of
NADPH. This protection is believed to occur through electron tunneling between NADPH on
the surface of the catalase and the heme group within the enzyme. The present study
provided additional support for the concept of an intermediate state of catalase, through …