Abstract

For many years, myoglobin was considered as an intracellular globin involved in oxygen transport and storage in cardiac and skeletal muscles. Following the discovery of its ability to convert nitrite into nitric oxide during hypoxia, myoglobin was shown to play a new role in the hypoxic signaling pathway that regulates mitochondrial functions of the electron-transport chain. This review presents experimental evidence that supports this concept and discusses the significance of this newly reported ability for cardiac and skeletal muscle functions.

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