The possible enzymatic activities of neuro- and cytoglobin as well as their potential function as substrates in enzymatic reactions were studied. Neuro- and cytoglobin are found to show no appreciable superoxide dismutase, catalase, and peroxidase activities. However, the internal disulfide bond (CD7-D5) of human neuroglobin can be reduced by thioredoxin reductase. Furthermore, our in vivo and in vitro studies show that Escherichia coli cells contain an enzymatic reducing system that keeps the heme iron atom of neuroglobin in the Fe2+ form in the presence of dioxygen despite the high autoxidation rate of the molecule. This reducing system needs a low-molecular-weight compound as co-factor. In vitro tests show that both NADH and NADPH can play this role. Furthermore, the reducing system is not specific for neuroglobin but allows the reduction of the ferric forms of other globins such as cytoglobin and myoglobin. A similar reducing system is present in eukaryotic tissue protein extracts. (c) 2007 Elsevier B.V. All rights reserved.

Neuroglobin and cytoglobin as potential enzyme or substrate / F., Trandafir; D., Hoogewijs; Altieri, Fabio; P., Rivetti Di Val Cervo; K., Ramser; S., Van Doorslaer; J. R., Vanfleteren; L., Moens; S., Dewilde. - In: GENE. - ISSN 0378-1119. - STAMPA. - 398:1-2 SPEC. ISS.(2007), pp. 103-113. (Intervento presentato al convegno 14th International Conference on Dioxygen Binding and Sensing Proteins tenutosi a Naples, ITALY nel SEP 03-07, 2006) [10.1016/j.gene.2007.02.038].

Neuroglobin and cytoglobin as potential enzyme or substrate

ALTIERI, Fabio;
2007

Abstract

The possible enzymatic activities of neuro- and cytoglobin as well as their potential function as substrates in enzymatic reactions were studied. Neuro- and cytoglobin are found to show no appreciable superoxide dismutase, catalase, and peroxidase activities. However, the internal disulfide bond (CD7-D5) of human neuroglobin can be reduced by thioredoxin reductase. Furthermore, our in vivo and in vitro studies show that Escherichia coli cells contain an enzymatic reducing system that keeps the heme iron atom of neuroglobin in the Fe2+ form in the presence of dioxygen despite the high autoxidation rate of the molecule. This reducing system needs a low-molecular-weight compound as co-factor. In vitro tests show that both NADH and NADPH can play this role. Furthermore, the reducing system is not specific for neuroglobin but allows the reduction of the ferric forms of other globins such as cytoglobin and myoglobin. A similar reducing system is present in eukaryotic tissue protein extracts. (c) 2007 Elsevier B.V. All rights reserved.
2007
catalase activity; peroxidase activity; reductase; thioredoxin reductase
01 Pubblicazione su rivista::01a Articolo in rivista
Neuroglobin and cytoglobin as potential enzyme or substrate / F., Trandafir; D., Hoogewijs; Altieri, Fabio; P., Rivetti Di Val Cervo; K., Ramser; S., Van Doorslaer; J. R., Vanfleteren; L., Moens; S., Dewilde. - In: GENE. - ISSN 0378-1119. - STAMPA. - 398:1-2 SPEC. ISS.(2007), pp. 103-113. (Intervento presentato al convegno 14th International Conference on Dioxygen Binding and Sensing Proteins tenutosi a Naples, ITALY nel SEP 03-07, 2006) [10.1016/j.gene.2007.02.038].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/75091
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