Important roles of Tyr43 at the putative heme distal side in the oxygen recognition and stability of the Fe(II)-O2 complex of YddV, a globin-coupled heme-based oxygen sensor diguanylate cyclase.

@article{Kitanishi2010ImportantRO,
  title={Important roles of Tyr43 at the putative heme distal side in the oxygen recognition and stability of the Fe(II)-O2 complex of YddV, a globin-coupled heme-based oxygen sensor diguanylate cyclase.},
  author={Kenichi Kitanishi and Kazuo Kobayashi and Yuriko Kawamura and Izumi Ishigami and Takashi Ogura and Kyosuke Nakajima and Jotaro Igarashi and Atsunari Tanaka and Toru Shimizu},
  journal={Biochemistry},
  year={2010},
  volume={49 49},
  pages={10381-93}
}
YddV from Escherichia coli (Ec) is a novel globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase activity in response to oxygen availability. In this study, we quantified the turnover numbers of the active [Fe(III), 0.066 min(-1); Fe(II)-O(2) and Fe(II)-CO, 0.022 min(-1)] [Fe(III), Fe(III)-protoporphyrin IX complex; Fe(II), Fe(II)-protoporphyrin IX complex] and inactive forms [Fe(II) and Fe(II)-NO, <0.01 min(-1)] of YddV for the first time. Our data indicate that the… CONTINUE READING

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