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

^*Corresponding author for this work

Institute of Physics

Johannes Gutenberg University Mainz

11 Citations (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.

Original language	English
Journal	Hyperfine Interactions
Volume	58
Issue number	1-4
Pages (from-to)	2405-2411
Number of pages	7
ISSN	0304-3843
DOIs	https://doi.org/10.1007/BF02398352
Publication status	Published - 01.07.1990

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title = "Recombination studies of photodissociated MbCO by M{\"o}ssbauer spectroscopy at low temperatures",

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.",

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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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