Ontology type: schema:ScholarlyArticle
2014-02-21
AUTHORSTrevor S. Kashey, John B. Cowgill, Michael D. McConnell, Marco Flores, Kevin E. Redding
ABSTRACTCytochrome c553 of Heliobacterium modesticaldum is the donor to P800+, the primary electron donor of the heliobacterial reaction center (HbRC). It is a membrane-anchored 14-kDa cytochrome that accomplishes electron transfer from the cytochrome bc complex to the HbRC. The petJ gene encoding cyt c553 was cloned and expressed in Escherichia coli with a hexahistidine tag replacing the lipid attachment site to create a soluble donor that could be made in a preparative scale. The recombinant cytochrome had spectral characteristics typical of a c-type cytochrome, including an asymmetric α-band, and a slightly red-shifted Soret band when reduced. The EPR spectrum of the oxidized protein was characteristic of a low-spin cytochrome. The midpoint potential of the recombinant cytochrome was +217 ± 10 mV. The interaction between soluble recombinant cytochrome c553 and the HbRC was also studied. Re-reduction of photooxidized P800+ was accelerated by addition of reduced cytochrome c553. The kinetics were characteristic of a bimolecular reaction with a second order rate of 1.53 × 104 M−1 s−1 at room temperature. The rate manifested a steep temperature dependence, with a calculated activation energy of 91 kJ mol−1, similar to that of the native protein in Heliobacillus gestii cells. These data demonstrate that the recombinant soluble cytochrome is comparable to the native protein, and likely lacks a discrete electrostatic binding site on the HbRC. More... »
PAGES291-299
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DOIhttp://dx.doi.org/10.1007/s11120-014-9982-y
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/24557489
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