TY - JOUR
T1 - Mössbauer spectroscopy on oxygenated sperm whale myoglobin
T2 - Evidence for an Fe3+O2 -coupling at the active center
AU - Bade, D.
AU - Parak, F.
N1 - Funding Information:
This work was supported by the Deutsche Forschungsgemeinschaft. We are indebted to Professors R. L. Mössbauer and G. M. Kalvius for their continuous support of this work.
PY - 1978
Y1 - 1978
N2 - 57Fe Mössbauer spectra of oxygenated sperm whale myoglobin (MbO2) show a well resolved quadrupole doublet with a temperature dependent splitting. The temperature dependence of the corresponding electric field gradient tensor (EFG) can be calculated from a Fe3+ term scheme for the iron at the active center. The Mössbauer spectra as well as the diamagnetic character of the MbO2-complex are then understood by an exchange coupling of the Fe3+-ion with the O2 - oxygen molecule ion. The resulting groundstate is a diamagnetic singlet. In order to keep the whole complex diamagnetic at room temperature, an exchange coupling with |Ј|⪴300cm-1is necessary. As the whole model is in fair agreement with many other spectroscopic data, it is believed to be a good starting point for further detailed calculations.
AB - 57Fe Mössbauer spectra of oxygenated sperm whale myoglobin (MbO2) show a well resolved quadrupole doublet with a temperature dependent splitting. The temperature dependence of the corresponding electric field gradient tensor (EFG) can be calculated from a Fe3+ term scheme for the iron at the active center. The Mössbauer spectra as well as the diamagnetic character of the MbO2-complex are then understood by an exchange coupling of the Fe3+-ion with the O2 - oxygen molecule ion. The resulting groundstate is a diamagnetic singlet. In order to keep the whole complex diamagnetic at room temperature, an exchange coupling with |Ј|⪴300cm-1is necessary. As the whole model is in fair agreement with many other spectroscopic data, it is believed to be a good starting point for further detailed calculations.
KW - Mössbauer Spectroscopy
KW - Oxygenated Myoglobin
UR - http://www.scopus.com/inward/record.url?scp=0017902203&partnerID=8YFLogxK
U2 - 10.1515/znc-1978-7-806
DO - 10.1515/znc-1978-7-806
M3 - Article
C2 - 152002
AN - SCOPUS:0017902203
SN - 0939-5075
VL - 33
SP - 488
EP - 494
JO - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
JF - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
IS - 7-8
ER -