ArticlePhotosynthesis research2009
Overexpression, characterization, and crystallization of the functional domain of cytochrome c(z) from Chlorobium tepidum.
Article in Photosynthesis research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Soluble domains of cytochromeCurrent research in structural biology · 2023Article
- The roles of C-terminal residues on the thermal stability and local heme environment of cytochrome c' from the thermophilic purple sulfur bacterium Thermochromatium tepidum.Photosynthesis research · 2015Article
- Structure analysis and characterization of the cytochrome c-554 from thermophilic green sulfur photosynthetic bacterium Chlorobaculum tepidum.Photosynthesis research · 2013Article
- Functional dissection of the multi-domain di-heme cytochrome c(550) from Thermus thermophilus.PloS one · 2013Article
- A sulfite respiration pathway from Thermus thermophilus and the key role of newly identified cytochrome c₅₅₀.Journal of bacteriology · 2011Article
- C-type cytochromes in the photosynthetic electron transfer pathways in green sulfur bacteria and heliobacteria.Photosynthesis research · 2010Review
- The chlorosome: a prototype for efficient light harvesting in photosynthesis.Photosynthesis research · 2010Review
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome c(z) is found in green sulfur photosynthetic bacteria, and is considered to be the only electron donor to the special pair P840 of the reaction center. It consists of an N-terminal transmembrane domain and a C-terminal soluble domain that binds a single heme group. Large scale expression of the C-terminal functional domain of the cytochrome c(z) (C-cyt c(z)) from the thermophilic bacterium Chlorobium tepidum has been achieved using the Escherichia coli expression system. The C-cyt c(z) expressed has been highly purified, and is stable at room temperature over 10 days of incubation for both reduced and oxidized forms. Spectroscopic measurements indicate that the heme iron in C-cyt c(z) is in a low-spin state and this does not change with the redox state. (1)H-NMR spectra of the oxidized C-cyt c(z) exhibited unusually large paramagnetic chemical shifts for the heme methyl protons in comparison with those of other Class I ferric cytochromes c. Differences in the (1)H-NMR linewidth were observed for some resonances, indicating different dynamic environments for these protons. Crystals of the oxidized C-cyt c(z) were obtained using ammonium sulfate as a precipitant. The crystals diffracted X-rays to a maximum resolution of 1.2 A, and the diffraction data were collected to 1.3 A resolution.
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