Literature DB >> 1504243

Spectral hole burning study of protoporphyrin IX substituted myoglobin.

J Zollfrank1, J Friedrich, F Parak.   

Abstract

Protoporphyrin IX substituted myoglobin reveals excellent hole burning properties. We investigated the frequency shift of persistent spectral holes under isotropic pressure conditions in a range from 0 to 2.4 MPa. In this range, the protein behaves like an elastic solid. The shift of the holes under pressure shows a remarkable frequency dependence from which the compressibility of the protein can be determined. The compressibility, in turn, allows for an estimation of the equilibrium volume fluctuations. Within the frame of the model used to interpret the pressure data, it is possible to determine the absorption frequency of the isolated chromophore and the associated solvent shift in the protein environment.

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Year:  1992        PMID： 1504243      PMCID： PMC1260289          DOI： 10.1016/S0006-3495(92)81876-3

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


  16 in total

1.  Glassy behavior of a protein.

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Journal:  Phys Rev Lett       Date:  1989-04-17       Impact factor: 9.161

2.  Thermodynamic fluctuations in protein molecules.

Authors:  A Cooper
Journal:  Proc Natl Acad Sci U S A       Date:  1976-08       Impact factor: 11.205

3.  Contributions of the electrostatic and the dispersion interaction to the solvent shift in a dye-polymer system, as investigated by hole-burning spectroscopy.

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Journal:  Phys Rev B Condens Matter       Date:  1990-06-15

4.  Spectroscopic studies of impurity-host interactions in dye-doped polymers: Hydrostatic-pressure effects versus temperature effects.

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Journal:  Phys Rev B Condens Matter       Date:  1987-11-15

5.  Low temperature X-ray investigation of structural distributions in myoglobin.

Authors:  F Parak; H Hartmann; K D Aumann; H Reuscher; G Rennekamp; H Bartunik; W Steigemann
Journal:  Eur Biophys J       Date:  1987       Impact factor: 1.733

6.  Low temperature photodissociation of hemoproteins: carbon monoxide complex of myoglobin and hemoglobin.

Authors:  T Iizuka; H Yamamoto; M Kotani; T Yonetani
Journal:  Biochim Biophys Acta       Date:  1974-11-05

7.  Conformational substates and motions in myoglobin. External influences on structure and dynamics.

Authors:  M K Hong; D Braunstein; B R Cowen; H Frauenfelder; I E Iben; J R Mourant; P Ormos; R Scholl; A Schulte; P J Steinbach
Journal:  Biophys J       Date:  1990-08       Impact factor: 4.033

8.  Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase.

Authors:  J Zollfrank; J Friedrich; J M Vanderkooi; J Fidy
Journal:  Biophys J       Date:  1991-02       Impact factor: 4.033

9.  More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. High resolution optical spectroscopic study.

Authors:  J Fidy; J M Vanderkooi; J Zollfrank; J Friedrich
Journal:  Biophys J       Date:  1992-02       Impact factor: 4.033

10.  Conformation-controlled trans-effect of the proximal histidine in haemoglobins. An electron spin resonance study of monomeric nitrosyl-57Fe-haemoglobins.

Authors:  M Overkamp; H Twilfer; K Gersonde
Journal:  Z Naturforsch C Biosci       Date:  1976 Sep-Oct
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  10 in total

1.  Stability diagram and unfolding of a modified cytochrome c: what happens in the transformation regime?

Authors:  Harald Lesch; Hans Stadlbauer; Josef Friedrich; Jane M Vanderkooi
Journal:  Biophys J       Date:  2002-03       Impact factor: 4.033

2.  Spectral hole burning and selection of conformational substates in chromoproteins.

Authors:  J Friedrich; J Gafert; J Zollfrank; J Vanderkooi; J Fidy
Journal:  Proc Natl Acad Sci U S A       Date:  1994-02-01       Impact factor: 11.205

3.  Softening of the packing density of horseradish peroxidase by a H-donor bound near the heme pocket.

Authors:  J Fidy; J M Vanderkooi; J Zollfrank; J Friedrich
Journal:  Biophys J       Date:  1992-12       Impact factor: 4.033

4.  High pressure studies of energy transfer and strongly coupled bacteriochlorophyll dimers in photosynthetic protein complexes.

Authors:  N R Reddy; H M Wu; R Jankowiak; R Picorel; R J Cogdell; G J Small
Journal:  Photosynth Res       Date:  1996-05       Impact factor: 3.573

5.  The enzyme horseradish peroxidase is less compressible at higher pressures.

Authors:  László Smeller; Judit Fidy
Journal:  Biophys J       Date:  2002-01       Impact factor: 4.033

6.  Ligand binding to heme proteins. V. Light-induced relaxation in proximal mutants L89I and H97F of carbonmonoxymyoglobin.

Authors:  Y Abadan; E Y Chien; K Chu; C D Eng; G U Nienhaus; S G Sligar
Journal:  Biophys J       Date:  1995-06       Impact factor: 4.033

7.  Pressure effects on the proximal heme pocket in myoglobin probed by Raman and near-infrared absorption spectroscopy.

Authors:  O Galkin; S Buchter; A Tabirian; A Schulte
Journal:  Biophys J       Date:  1997-11       Impact factor: 4.033

8.  Interpretation of multiple Q(0,0) bands in the absorption spectrum of Mg-mesoporphyrin embedded in horseradish peroxidase.

Authors:  E Balog; K Kis-Petik; J Fidy; M Köhler; J Friedrich
Journal:  Biophys J       Date:  1997-07       Impact factor: 4.033

9.  Mössbauer spectroscopy on nonequilibrium states of myoglobin: a study of r-t relaxation.

Authors:  V E Prusakov; J Steyer; F G Parak
Journal:  Biophys J       Date:  1995-06       Impact factor: 4.033

10.  Dissimilar flexibility of α and β subunits of human adult hemoglobin influences the protein dynamics and its alteration induced by allosteric effectors.

Authors:  Gusztáv Schay; András D Kaposi; László Smeller; Krisztián Szigeti; Judit Fidy; Levente Herenyi
Journal:  PLoS One       Date:  2018-03-27       Impact factor: 3.240
  10 in total

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