Low temperature study of myoglobin-ligand rebinding kinetics with Mossbauer spectroscopy

C. Ober; M. Burkardt; H. Winkler; A. X. Trautwein; A. A. Zharikov; S. F. Fischer; F. Parak

doi:10.1007/s002490050075

Low temperature study of myoglobin-ligand rebinding kinetics with Mossbauer spectroscopy

C. Ober, M. Burkardt, H. Winkler, A. X. Trautwein^*, A. A. Zharikov, S. F. Fischer, F. Parak

^*Corresponding author for this work

6 Citations (Scopus)

Abstract

We have studied the recombination kinetics of carboxymyoglobin (after photodissociation of the CO ligand) by Mossbauer spectroscopy for temperatures in the range 4.2-60 K. The observed kinetics display non-exponential behaviour which was monitored over periods of a few days. It is shown that the time dependence of the kinetics can be reduced to a single universal function of the temperature-dependent variable (t/τ(1/2)(T))(β(T)). The half-decay time τ(1/2)(T) and the scaling parameter β(T) are analysed for the presence of tunneling effects. The non-Arrhenius temperature dependence of the half-decay time below 60 K is interpreted as activated tunneling in models with an Eckart barrier or a fluctuating barrier.

Original language	English
Journal	European Biophysics Journal
Volume	26
Issue number	3
Pages (from-to)	227-237
Number of pages	11
ISSN	0175-7571
DOIs	https://doi.org/10.1007/s002490050075
Publication status	Published - 01.01.1997

Funding

Acknowledgement This work was supported by the Deutsche For-schungsgemeinschaft (SFB 143 and SFB 377) and by an European Union Human Capital and Mobility grant to the MASIMO network (ERBCHRX CT-920072).

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title = "Low temperature study of myoglobin-ligand rebinding kinetics with Mossbauer spectroscopy",

abstract = "We have studied the recombination kinetics of carboxymyoglobin (after photodissociation of the CO ligand) by Mossbauer spectroscopy for temperatures in the range 4.2-60 K. The observed kinetics display non-exponential behaviour which was monitored over periods of a few days. It is shown that the time dependence of the kinetics can be reduced to a single universal function of the temperature-dependent variable (t/τ(1/2)(T))(β(T)). The half-decay time τ(1/2)(T) and the scaling parameter β(T) are analysed for the presence of tunneling effects. The non-Arrhenius temperature dependence of the half-decay time below 60 K is interpreted as activated tunneling in models with an Eckart barrier or a fluctuating barrier.",

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T1 - Low temperature study of myoglobin-ligand rebinding kinetics with Mossbauer spectroscopy

AU - Ober, C.

AU - Burkardt, M.

AU - Winkler, H.

AU - Trautwein, A. X.

AU - Zharikov, A. A.

AU - Fischer, S. F.

AU - Parak, F.

PY - 1997/1/1

Y1 - 1997/1/1

N2 - We have studied the recombination kinetics of carboxymyoglobin (after photodissociation of the CO ligand) by Mossbauer spectroscopy for temperatures in the range 4.2-60 K. The observed kinetics display non-exponential behaviour which was monitored over periods of a few days. It is shown that the time dependence of the kinetics can be reduced to a single universal function of the temperature-dependent variable (t/τ(1/2)(T))(β(T)). The half-decay time τ(1/2)(T) and the scaling parameter β(T) are analysed for the presence of tunneling effects. The non-Arrhenius temperature dependence of the half-decay time below 60 K is interpreted as activated tunneling in models with an Eckart barrier or a fluctuating barrier.

AB - We have studied the recombination kinetics of carboxymyoglobin (after photodissociation of the CO ligand) by Mossbauer spectroscopy for temperatures in the range 4.2-60 K. The observed kinetics display non-exponential behaviour which was monitored over periods of a few days. It is shown that the time dependence of the kinetics can be reduced to a single universal function of the temperature-dependent variable (t/τ(1/2)(T))(β(T)). The half-decay time τ(1/2)(T) and the scaling parameter β(T) are analysed for the presence of tunneling effects. The non-Arrhenius temperature dependence of the half-decay time below 60 K is interpreted as activated tunneling in models with an Eckart barrier or a fluctuating barrier.

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DO - 10.1007/s002490050075

M3 - Journal articles

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JO - European Biophysics Journal

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IS - 3

ER -

Low temperature study of myoglobin-ligand rebinding kinetics with Mossbauer spectroscopy

Abstract

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