Biophysical applications

A. X. Trautwein; H. Winkler

doi:10.1023/A:1017036326459

Biophysical applications

A. X. Trautwein^*, H. Winkler

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Physik

5 Zitate (Scopus)

Abstract

Nuclear forward scattering (NFS) of synchrotron radiation was applied to investigate the electronic and magnetic properties of (i) the diamagnetic "picket-fence" porphyrin FeO₂(SC₆HF₄)(TP_pivP), which is a model for oxygenated hemoglobin and myoglobin and (ii) the paramagnetic "picket-fence" porphyrin [Fe(CH₃COOH)(TP_pivP)]^-, which is a model for the ferrous state of the prosthetic group, termed P460, of the multi-heme enzyme hydroxylamine oxidoreductase from the bacterium Nitrosomonas europeae.

Originalsprache	Englisch
Zeitschrift	Hyperfine Interactions
Jahrgang	123-124
Ausgabenummer	1-4
Seiten (von - bis)	561-570
Seitenumfang	10
ISSN	0304-3843
DOIs	https://doi.org/10.1023/A:1017036326459
Publikationsstatus	Veröffentlicht - 01.12.1999

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year = "1999",

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doi = "10.1023/A:1017036326459",

language = "English",

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T1 - Biophysical applications

AU - Trautwein, A. X.

AU - Winkler, H.

PY - 1999/12/1

Y1 - 1999/12/1

N2 - Nuclear forward scattering (NFS) of synchrotron radiation was applied to investigate the electronic and magnetic properties of (i) the diamagnetic "picket-fence" porphyrin FeO2(SC6HF4)(TPpivP), which is a model for oxygenated hemoglobin and myoglobin and (ii) the paramagnetic "picket-fence" porphyrin [Fe(CH3COOH)(TPpivP)]-, which is a model for the ferrous state of the prosthetic group, termed P460, of the multi-heme enzyme hydroxylamine oxidoreductase from the bacterium Nitrosomonas europeae.

AB - Nuclear forward scattering (NFS) of synchrotron radiation was applied to investigate the electronic and magnetic properties of (i) the diamagnetic "picket-fence" porphyrin FeO2(SC6HF4)(TPpivP), which is a model for oxygenated hemoglobin and myoglobin and (ii) the paramagnetic "picket-fence" porphyrin [Fe(CH3COOH)(TPpivP)]-, which is a model for the ferrous state of the prosthetic group, termed P460, of the multi-heme enzyme hydroxylamine oxidoreductase from the bacterium Nitrosomonas europeae.

UR - https://www.scopus.com/pages/publications/0013322798

U2 - 10.1023/A:1017036326459

DO - 10.1023/A:1017036326459

M3 - Journal articles

AN - SCOPUS:0013322798

SN - 0304-3843

VL - 123-124

SP - 561

EP - 570

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Biophysical applications

Abstract

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