Oxygen and temperature-dependent structural and redox changes in a novel cytochrome c4 from the purple sulfur photosynthetic bacterium Thiocapsa roseopersicina
Section snippets
Experimental procedures
Thiocapsa roseopersicina was grown under standard photosynthetic conditions as described earlier [16]. Cells were harvested in the logarithmic phase of growth and were stored at −20 °C.
Molecular mass and heme content of cytochrome
We have purified and identified three cytochromes from T. roseopersicina: a flavocytochrome c with two subunits (22 and 42 kDa), which is probably the same as described earlier [33], and two cytochromes with only one peptide chain. We used the larger cytochrome monomer in this study which displayed only one band on SDS gradient PAGE, at a molecular mass of ∼25 kDa. Recently, we have determined the exact mass by mass spectrometry; 21582 Da [34]. This unit contains two hemes per molecule, as
Classification of the cytochrome c4 from T. roseopersicina
Four different cytochromes have been purified and characterized from T. roseopersicina so far [33], [41], [42], [43]. The cytochrome c4 presented in this paper is different from any of the previously purified ones.
Three of the reported cytochromes from T. roseopersicina have substantially higher (55 kDa [42] and 180 kDa [41]) or lower (4∗11 kDa [43]) molecular masses than that of cytochrome c4. The flavocytochrome c552 from T. roseopersicina[33] possesses a di-heme subunit with a similar mass (∼21
Acknowledgments
We are grateful for the financial support of the Hungarian Science Foundation [OTKA T049276 and OTKA T049207] and AUTOESKORT Ltd. Rui M.M. Branca acknowledges the financial support of the Portuguese Science and Technology Foundation under the PhD fellowship of POCTI, SFRH/BD/13128/2003.
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