Recombination studies of photodissociated MbCO by Mössbauer spectroscopy at low temperatures

H. Winkler; M. Franke; A. X. Trautwein; F. Parak

doi:10.1007/BF02398352

Recombination studies of photodissociated MbCO by Mössbauer spectroscopy at low temperatures

H. Winkler^*, M. Franke, A. X. Trautwein, F. Parak

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

Institut für Physik

Johannes Gutenberg-Universität Mainz

11 Zitate (Scopus)

Abstract

Rebinding of carbonmonoxide to myoglobin after photodissociation has been studied by Mössbauer spectroscopy at 57.6 K and below for up to 9 days. The time dependence is reproduced by a set of exponentials representing a distribution of activation enthalpies. A shift to smaller values of these activation enthalpies and of the preexponential factor compared to optical studies at higher temperatures has been observed as well as pumping into long-living states.

Originalsprache	Englisch
Zeitschrift	Hyperfine Interactions
Jahrgang	58
Ausgabenummer	1-4
Seiten (von - bis)	2405-2411
Seitenumfang	7
ISSN	0304-3843
DOIs	https://doi.org/10.1007/BF02398352
Publikationsstatus	Veröffentlicht - 01.07.1990

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abstract = "Rebinding of carbonmonoxide to myoglobin after photodissociation has been studied by M{\"o}ssbauer spectroscopy at 57.6 K and below for up to 9 days. The time dependence is reproduced by a set of exponentials representing a distribution of activation enthalpies. A shift to smaller values of these activation enthalpies and of the preexponential factor compared to optical studies at higher temperatures has been observed as well as pumping into long-living states.",

author = "H. Winkler and M. Franke and Trautwein, \{A. X.\} and F. Parak",

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T1 - Recombination studies of photodissociated MbCO by Mössbauer spectroscopy at low temperatures

AU - Winkler, H.

AU - Franke, M.

AU - Trautwein, A. X.

AU - Parak, F.

PY - 1990/7/1

Y1 - 1990/7/1

N2 - Rebinding of carbonmonoxide to myoglobin after photodissociation has been studied by Mössbauer spectroscopy at 57.6 K and below for up to 9 days. The time dependence is reproduced by a set of exponentials representing a distribution of activation enthalpies. A shift to smaller values of these activation enthalpies and of the preexponential factor compared to optical studies at higher temperatures has been observed as well as pumping into long-living states.

AB - Rebinding of carbonmonoxide to myoglobin after photodissociation has been studied by Mössbauer spectroscopy at 57.6 K and below for up to 9 days. The time dependence is reproduced by a set of exponentials representing a distribution of activation enthalpies. A shift to smaller values of these activation enthalpies and of the preexponential factor compared to optical studies at higher temperatures has been observed as well as pumping into long-living states.

UR - https://www.scopus.com/pages/publications/0011498529

U2 - 10.1007/BF02398352

DO - 10.1007/BF02398352

M3 - Journal articles

AN - SCOPUS:0011498529

SN - 0304-3843

VL - 58

SP - 2405

EP - 2411

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Recombination studies of photodissociated MbCO by Mössbauer spectroscopy at low temperatures

Abstract

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