Photophysical properties of cytochromes c-553 and c3 extracted from Desulfovibrio vulgaris Miyazaki
| Autor: | Toshihiko Nagamura, Miriam Abe, Tatsuhiko Yagi, Hideyuki Itagaki |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Hemeprotein
biology Cytochrome General Chemical Engineering Cytochrome c Fluorescence spectrometry General Physics and Astronomy General Chemistry biology.organism_classification Photochemistry Porphyrin chemistry.chemical_compound Crystallography chemistry biology.protein Desulfovibrio vulgaris Heme Hemin |
| Zdroj: | Journal of Photochemistry and Photobiology A: Chemistry. 120:125-133 |
| ISSN: | 1010-6030 |
| DOI: | 10.1016/s1010-6030(98)00420-1 |
| Popis: | Fluorescence and UV/visible absorption properties were studied on electron carrier proteins cytochromes c -553 and c 3 and their Fe-free forms (Fe-free cytochromes) over wide pH and temperature ranges in comparison with cytochrome c , hemin and microperoxidase-9 (MP-9). Although cytochromes c -553 and c 3 were extracted from the same sulfate-reducing bacterium, their absorption spectra at acidic pH and pH dependence of fluorescence spectra were different. Cytochrome c -553 showed photophysical characteristics similar to cytochrome c . This is attributed to the influence of the ligands of the fifth and sixth positions of the heme iron in cytochromes c -553 and c 3 , which was confirmed by the experiments on MP-9. Through the temperature-dependent fluorescence spectrum and time profile, the coexistence of protonated and deprotonated forms of Fe-free cytochromes at neutral pH was observed. The fluorescence in native cytochromes was observed at acidic pH, whereas MP-9 and hemin showed no fluorescence at the same condition. |
| Databáze: | OpenAIRE |
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