Reactive complexes in myoglobin and nitric oxide synthase

Hans Petter Hersleth, Armelle Varnier, Espen Harbitz, Åsmund Kjendseth Røhr, Peter P. Schmidt, Morten Sørlie, F. Henning Cederkvist, Stéphane Marchal, Antonius C.F. Gorren, Bernd Mayer, Takeshi Uchida, Volker Schünemann, Teizo Kitagawa, Alfred X. Trautwein, Toru Shimizu, Reinhard Lange, Carl Henrik Görbitz, K. Kristoffer Andersson*

*Corresponding author for this work
7 Citations (Scopus)


In this overview some of our crystallographic and spectroscopic studies on reactive complexes in myoglobin and nitric oxide synthase are summarised. Myoglobin and nitric oxide synthase are both haemoproteins with some similar reaction intermediates. For myoglobin we have studied different intermediates generated in the reaction with hydrogen peroxide by X-ray diffraction, single-crystal microspectrophotometry, electron paramagnetic resonance spectroscopy, Mössbauer spectroscopy, resonance Raman spectroscopy and quantum refinement. Several of these myoglobin states are quite susceptible to radiation-induced changes during crystallographic data collection, and we have observed a radiation-induced change of the ferric resting myoglobin to aqua ferrous myoglobin, of myoglobin compound II to a proposed intermediate H, and of myoglobin compound III to peroxy myoglobin. For the myoglobin compound II/ intermediate H we observe a single-bonded FeIV-O species, which is probably protonated. The long Fe-O bond seen in the crystal structure can be supported by the observation of a new 18O-sensitive resonance Raman mode at 687 cm-1. For nitric oxide synthase we detected with cryobiochemical methods in electron paramagnetic resonance spectra the first biopterin radical serving as electron donor to the ferrous-oxy complex, and that biopterin serves as a proton donor as well, in addition we could observe formation of the Fe(NO) complex with a amino-pterin cofactor capable to form a reactive radical.

Original languageEnglish
JournalInorganica Chimica Acta
Issue number4
Pages (from-to)831-843
Number of pages13
Publication statusPublished - 03.03.2008


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