Interaction of cytochrome c
L with methanol dehydrogenase from Methylophaga marina 42: |
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Authors: | Irmgard Heiber-Langer Cécile Clery Johannes Franks Patrick Masson Claude Balny |
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Institution: | (1) Unitè 128, CNRS, Institut National de la Santé et de la Recherche Médicale, BP 5051, F-34033 Montpellier Cédex 1, France;(2) Unité de Biochimie, Centre de Recherches du Service de Santé des Armées, F-38702 La Tronche, France;(3) Kluyver Laboratory of Biotechnology, Technical University Delft, Julianalaan 67, NL-2628 BC Delft, The Netherlands;(4) U128, CNRS, Institut National de la Santé et de la Recherche Médicale, BP 5051, F-34033 Montpellier Cédex 1, France |
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Abstract: | The reaction of methanol dehydrogenase with cytochrome c
L from Methylophaga marina and the reactions of the non-physiological substrates, Wurster's blue and ascorbic acid, with both proteins were studied as a function of temperature (4–32 °C), pressure (1–2000 bar) and ionic strength using the optical high pressure stopped-flow method. The thermodynamic parameters H, S and V were determined for all reactions where electron transfers are involved. These data allowed the determination of the Maxwell relationships which proved the internal thermodynamic consistency of the system under study. A conformational change on the cytochrome c
L level was deduced from both breaks in the Arrhenius plots and the variation of the V with temperature.Abbreviations MOPS
4-morpholinepropanesulfonic acid
- CHES
2-(cyclohexylamino)ethanesulfonic acid
- MDH
methanol dehydrogenase
- EDTA
ethylenedinitrilotetraacetic acid disodium salt
- BTB
bromothymol blue (3,3-dibromothymolsulfoneph-thalein)
- PQQ
2,7,9-tricarboxy-lH-pyrrolo-2,3f]quinoline-4,5-dione
- cytochrome c
HH
mammalian horse heart cytochrome c |
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Keywords: | Methanol dehydrogenase Cytochrome c
L Electron transfer High pressure stopped-flow Hydrostatic pressure High pressure electrophoresis |
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