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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Busch, Manuela Mäntele, Werner Stumpp, Tina V. M. Cenacchi, Lucia Müller, Florian G. Schleidt, Philipp G. Trost, Paolo Lancaster, C. Roy D. |
| Description | Author Affiliation: Cenacchi L ( Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, Frankfurt, Germany.) |
| Abstract | Cytochrome (cyt) $b_{561}$ proteins are dihaem-containing membrane proteins, belonging to the CYBASC $(cytochrome-b_{561}-ascorbate-reducible)$ family, and are proposed to be involved in ascorbate recycling and/or the facilitation of iron absorption. Here, we present the heterologous production of two cyt $b_{561}$ paralogs from Arabidopsis thaliana $(Acytb_{561}-A,$ $Acytb_{561}-B)$ in Escherichia coli and Pichia pastoris, their purification, and initial characterisation. Spectra indicated that $Acytb_{561}-A$ resembles the best characterised member of the CYBASC family, the cytochrome $b_{561}$ from adrenomedullary chromaffin vesicles, and that $Acytb_{561}-B$ is atypical compared to other CYBASC proteins. Haem oxidation–reduction midpoint potential $(E_{M})$ values were found to be fully consistent with ascorbate oxidation activities and $Fe^{3 +}-chelates$ reductase activities. The ascorbate dependent reduction and protein stability of both paralogs were found to be sensitive to alkaline pH values as reported for the cytochrome $b_{561}$ from chromaffin vesicles. For both paralogs, ascorbate-dependent reduction was inhibited and the low-potential haem $E_{M}$ values were affected significantly by incubation with diethyl pyrocarbonate (DEPC) in the absence of ascorbate. Modification with DEPC in the presence of ascorbate left the haem $E_{M}$ values unaltered compared to the unmodified proteins. However, ascorbate reduction was inhibited. We concluded that the ascorbate-binding site is located near the low-potential haem with the $Fe^{3 +}-chelates$ reduction-site close to the high-potential haem. Furthermore, inhibition of ascorbate oxidation by DEPC treatment occurs not only by lowering the haem $E_{M}$ values but also by an additional modification affecting ascorbate binding and/or electron transfer. Analytical gel filtration experiments suggest that both cyt $b_{561}$ paralogs exist as homodimers. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 3 |
| Volume Number | 1818 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-03-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Arabidopsis Proteins Biosynthesis Arabidopsis Enzymology Cytochrome b Group Escherichia Coli Fungal Proteins Pichia Recombinant Proteins Genetics Chemistry Ascorbic Acid Diethyl Pyrocarbonate Electron Transport Gene Expression Heme Oxidation-Reduction Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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