Abstract
Substitution of H2 16O by H2 17O induces a substantial broadening of the high-field line in the electron-spin resonance spectrum of ferric myoglobin due to the presence of H2 17O at the axial ligand-site. Computer simulations of the experimental spectra yielded the values of the reciprocal relaxation time T2 -1 = 7.8 G and the 17O-hyperfine coupling constant A = 18 ± 1 G. Under identical experimental conditions no effect of H2 17O was observed in horseradish peroxidase. The latter finding excludes the possibility that a water molecule is liganded to the peroxidase haem-iron and supports either the idea that both axial ligands are amino acid residues or that the haem in ferric horseradish peroxidase is pentacoordinate.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 885-889 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 79 |
| Issue number | 3 |
| DOIs | |
| State | Published - Dec 7 1977 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Probing axial ligands in ferric haemoproteins : An ESR study of myoglobin and horseradish peroxidase in H2 17O. / Vuk-Pavlović, S.; Siderer, Y.
In: Biochemical and Biophysical Research Communications, Vol. 79, No. 3, 07.12.1977, p. 885-889.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Probing axial ligands in ferric haemoproteins
T2 - An ESR study of myoglobin and horseradish peroxidase in H2 17O
AU - Vuk-Pavlović, S.
AU - Siderer, Y.
PY - 1977/12/7
Y1 - 1977/12/7
N2 - Substitution of H2 16O by H2 17O induces a substantial broadening of the high-field line in the electron-spin resonance spectrum of ferric myoglobin due to the presence of H2 17O at the axial ligand-site. Computer simulations of the experimental spectra yielded the values of the reciprocal relaxation time T2 -1 = 7.8 G and the 17O-hyperfine coupling constant A = 18 ± 1 G. Under identical experimental conditions no effect of H2 17O was observed in horseradish peroxidase. The latter finding excludes the possibility that a water molecule is liganded to the peroxidase haem-iron and supports either the idea that both axial ligands are amino acid residues or that the haem in ferric horseradish peroxidase is pentacoordinate.
AB - Substitution of H2 16O by H2 17O induces a substantial broadening of the high-field line in the electron-spin resonance spectrum of ferric myoglobin due to the presence of H2 17O at the axial ligand-site. Computer simulations of the experimental spectra yielded the values of the reciprocal relaxation time T2 -1 = 7.8 G and the 17O-hyperfine coupling constant A = 18 ± 1 G. Under identical experimental conditions no effect of H2 17O was observed in horseradish peroxidase. The latter finding excludes the possibility that a water molecule is liganded to the peroxidase haem-iron and supports either the idea that both axial ligands are amino acid residues or that the haem in ferric horseradish peroxidase is pentacoordinate.
UR - http://www.scopus.com/inward/record.url?scp=0017661254&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017661254&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(77)91193-7
DO - 10.1016/0006-291X(77)91193-7
M3 - Article
C2 - 202277
AN - SCOPUS:0017661254
VL - 79
SP - 885
EP - 889
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -