Article
The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.
Journal of the American Chemical Society - 23 Dec 2009
Yi Jun, Heinecke Julie, Tan Hui, Ford Peter C, Richter-Addo George B
Abstract excerpt
It is now well-established that mammalian heme proteins are reactive with various nitrogen oxide species and that these reactions may play significant roles in mammalian physiology. For example, the ferrous heme protein myoglobin (Mb) has been shown to reduce nitrite (NO(2)(-)) to nitric oxide (NO) under hypoxic conditions. We demonstrate here that the distal pocket histidine residue (His64) of horse heart...
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