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Research article - Peer-reviewed, 2005

NO binding to naphthalene dioxygenase

Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S


Nitric oxide (NO) is commonly used as an analogue for dioxygen in structural and spectroscopic studies of oxygen binding and oxygen activation. In this study, crystallographic structures of naphthalene dioxygenase (NDO) in complex with nitric oxide are reported. In the presence of the aromatic substrate indole, NO is bound end-on to the active-site mononuclear iron of NDO. The structural observations correlate well with spectroscopic measurements of NO binding to NDO in solution. However, the end-on binding of NO is in contrast to the recently reported structure of oxygen to the active-site iron of NDO that binds side-on. While NO is a good oxygen analogue with many similarities to O-2, the different binding mode of NO to the active-site iron atom leads to different mechanistic implications. Hence, caution needs to be used in extrapolating NO as an analogue to O-2 binding


Rieske dioxygenase - Nitric oxide - Iron - Crystal structures - Indole

Published in

Journal of Biological Inorganic Chemistry
2005, Volume: 10, number: 5, pages: 483-489
Publisher: SPRINGER

      SLU Authors

    • Karlsson Tiselius, Andreas

      • Department of Molecular Biology, Swedish University of Agricultural Sciences
      • Eklund, Hans

        • Department of Molecular Biology, Swedish University of Agricultural Sciences

      UKÄ Subject classification

      Environmental Sciences related to Agriculture and Land-use

      Publication Identifiers


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