Iron(II)-dioxygen interaction detected by Mössbauer and ESR spectroscopy

E. Bill; X. Q. Ding; C. Haas; H. Winkler; A. X. Trautwein; M. Zeppezauer

doi:10.1007/BF02395529

Iron(II)-dioxygen interaction detected by Mössbauer and ESR spectroscopy

E. Bill^*, X. Q. Ding, C. Haas, H. Winkler, A. X. Trautwein, M. Zeppezauer

^*Corresponding author for this work

Saarland University

1 Citation (Scopus)

Abstract

The electronic structure of Fe(II) substituting Zn in Horse Liver Alcohol Dehydrogenase was investigated by Mössbauer spectroscopy at various temperatures and applied magnetic fields and by spin Hamiltonian analysis of the results. The novelty we found, is an unusually weak spin coupling of Fe(II) with a diradical (S=1). From ESR results and biochemical findings we conclude, that the corresponding chemical species is triplet oxygen (O₂). Oxidation experiments, followed by Mössbauer spectroscopy, show that the spin-coupled species is an outer-sphere Fe(II)... O₂ complex occuring as an intermediate of the dioxygen activation reaction, catalysed by Fe(II). A second Fe(II)-O₂ complex could be detected, which corresponds to an inner-sphere complex with O₂ directly bound to iron. The spin hamiltonian parameters in the coupled system describing the electronic properties of iron are presented. The results are compared with those of iron in other nonheme iron proteins.

Original language	English
Journal	Hyperfine Interactions
Volume	42
Issue number	1-4
Pages (from-to)	877-880
Number of pages	4
ISSN	0304-3843
DOIs	https://doi.org/10.1007/BF02395529
Publication status	Published - 01.02.1988

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title = "Iron(II)-dioxygen interaction detected by M{\"o}ssbauer and ESR spectroscopy",

abstract = "The electronic structure of Fe(II) substituting Zn in Horse Liver Alcohol Dehydrogenase was investigated by M{\"o}ssbauer spectroscopy at various temperatures and applied magnetic fields and by spin Hamiltonian analysis of the results. The novelty we found, is an unusually weak spin coupling of Fe(II) with a diradical (S=1). From ESR results and biochemical findings we conclude, that the corresponding chemical species is triplet oxygen (O2). Oxidation experiments, followed by M{\"o}ssbauer spectroscopy, show that the spin-coupled species is an outer-sphere Fe(II)... O2 complex occuring as an intermediate of the dioxygen activation reaction, catalysed by Fe(II). A second Fe(II)-O2 complex could be detected, which corresponds to an inner-sphere complex with O2 directly bound to iron. The spin hamiltonian parameters in the coupled system describing the electronic properties of iron are presented. The results are compared with those of iron in other nonheme iron proteins.",

author = "E. Bill and Ding, {X. Q.} and C. Haas and H. Winkler and Trautwein, {A. X.} and M. Zeppezauer",

year = "1988",

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doi = "10.1007/BF02395529",

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journal = "Hyperfine Interactions",

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T1 - Iron(II)-dioxygen interaction detected by Mössbauer and ESR spectroscopy

AU - Bill, E.

AU - Ding, X. Q.

AU - Haas, C.

AU - Winkler, H.

AU - Trautwein, A. X.

AU - Zeppezauer, M.

PY - 1988/2/1

Y1 - 1988/2/1

N2 - The electronic structure of Fe(II) substituting Zn in Horse Liver Alcohol Dehydrogenase was investigated by Mössbauer spectroscopy at various temperatures and applied magnetic fields and by spin Hamiltonian analysis of the results. The novelty we found, is an unusually weak spin coupling of Fe(II) with a diradical (S=1). From ESR results and biochemical findings we conclude, that the corresponding chemical species is triplet oxygen (O2). Oxidation experiments, followed by Mössbauer spectroscopy, show that the spin-coupled species is an outer-sphere Fe(II)... O2 complex occuring as an intermediate of the dioxygen activation reaction, catalysed by Fe(II). A second Fe(II)-O2 complex could be detected, which corresponds to an inner-sphere complex with O2 directly bound to iron. The spin hamiltonian parameters in the coupled system describing the electronic properties of iron are presented. The results are compared with those of iron in other nonheme iron proteins.

AB - The electronic structure of Fe(II) substituting Zn in Horse Liver Alcohol Dehydrogenase was investigated by Mössbauer spectroscopy at various temperatures and applied magnetic fields and by spin Hamiltonian analysis of the results. The novelty we found, is an unusually weak spin coupling of Fe(II) with a diradical (S=1). From ESR results and biochemical findings we conclude, that the corresponding chemical species is triplet oxygen (O2). Oxidation experiments, followed by Mössbauer spectroscopy, show that the spin-coupled species is an outer-sphere Fe(II)... O2 complex occuring as an intermediate of the dioxygen activation reaction, catalysed by Fe(II). A second Fe(II)-O2 complex could be detected, which corresponds to an inner-sphere complex with O2 directly bound to iron. The spin hamiltonian parameters in the coupled system describing the electronic properties of iron are presented. The results are compared with those of iron in other nonheme iron proteins.

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DO - 10.1007/BF02395529

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SN - 0304-3843

VL - 42

SP - 877

EP - 880

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Iron(II)-dioxygen interaction detected by Mössbauer and ESR spectroscopy

Abstract

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