EPR characterization of axial bond in metal center of native and cobalt-substituted guanylate cyclase.

@article{Makino1999EPRCO,
  title={EPR characterization of axial bond in metal center of native and cobalt-substituted guanylate cyclase.},
  author={Ryu Makino and Hiroko Matsuda and Eiji Obayashi and Yoshitsugu Shiro and Tetsutaro Iizuka and Hiroshi Hori},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 12},
  pages={7714-23}
}
The nature of the metal-proximal base bond of soluble guanylate cyclase from bovine lung was examined by EPR spectroscopy. When the ferrous enzyme was mixed with NO, a new species was transiently produced and rapidly converted to a five-coordinate ferrous NO complex. The new species exhibited the EPR signal of six-coordinate ferrous NO complex with a feature of histidine-ligated heme. The histidine ligation was further examined by using the cobalt protoporphyrin IX-substituted enzyme. The Co2… CONTINUE READING

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