TY - JOUR
T1 - Reactive complexes in myoglobin and nitric oxide synthase
AU - Hersleth, Hans Petter
AU - Varnier, Armelle
AU - Harbitz, Espen
AU - Røhr, Åsmund Kjendseth
AU - Schmidt, Peter P.
AU - Sørlie, Morten
AU - Cederkvist, F. Henning
AU - Marchal, Stéphane
AU - Gorren, Antonius C.F.
AU - Mayer, Bernd
AU - Uchida, Takeshi
AU - Schünemann, Volker
AU - Kitagawa, Teizo
AU - Trautwein, Alfred X.
AU - Shimizu, Toru
AU - Lange, Reinhard
AU - Görbitz, Carl Henrik
AU - Andersson, K. Kristoffer
PY - 2008/3/3
Y1 - 2008/3/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=39049136395&partnerID=8YFLogxK
U2 - 10.1016/j.ica.2007.09.045
DO - 10.1016/j.ica.2007.09.045
M3 - Scientific review articles
AN - SCOPUS:39049136395
SN - 0020-1693
VL - 361
SP - 831
EP - 843
JO - Inorganica Chimica Acta
JF - Inorganica Chimica Acta
IS - 4
ER -