%0 Journal Article %1 citeulike:895360 %A Abe, Miriam %A Yagi, Tatsuhiko %A Itagaki, Hideyuki %A Nagamura, Toshihiko %D 1999 %J Journal of Photochemistry and Photobiology A: Chemistry %K fluorescence heme-protein heme iron uv p450 reference %N 2 %P 125--133 %R 10.1016/S1010-6030(98)00420-1 %T Photophysical properties of cytochromes c-553 and c3 extracted from Desulfovibrio vulgaris Miyazaki %U http://dx.doi.org/10.1016/S1010-6030(98)00420-1 %V 120 %X Fluorescence and UV/visible absorption properties were studied on electron carrier proteins cytochromes c-553 and c3 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 c3 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 c3, 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.

@article{citeulike:895360, abstract = {Fluorescence and UV/visible absorption properties were studied on electron carrier proteins cytochromes c-553 and c3 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 c3 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 c3, 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.}, added-at = {2007-02-02T11:54:15.000+0100}, author = {Abe, Miriam and Yagi, Tatsuhiko and Itagaki, Hideyuki and Nagamura, Toshihiko}, biburl = {https://www.bibsonomy.org/bibtex/262c8f0cb62662c8eda5abd79f0a5ff15/robert}, citeulike-article-id = {895360}, doi = {10.1016/S1010-6030(98)00420-1}, interhash = {faeb8c631b7d8bce97abcda95c65c55b}, intrahash = {62c8f0cb62662c8eda5abd79f0a5ff15}, journal = {Journal of Photochemistry and Photobiology A: Chemistry}, keywords = {fluorescence heme-protein heme iron uv p450 reference}, month = {January}, number = 2, pages = {125--133}, priority = {2}, timestamp = {2007-02-02T11:54:15.000+0100}, title = {Photophysical properties of cytochromes c-553 and c3 extracted from \textit{Desulfovibrio vulgaris Miyazaki}}, url = {http://dx.doi.org/10.1016/S1010-6030(98)00420-1}, volume = 120, year = 1999 }