Membrane-Associated c-type Cytochromes from the Green Sulfur Bacterium Chlorobium limicola forma thiosulfatophilum:  Purification and Characterization of Cytochrome c553

Albouy, Delphine; Sturgis, James N.; Feiler, Ute; Nitschke, Wolfgang; Robert, Bruno

doi:10.1021/bi962624g

Cited by 14 publications

(14 citation statements)

References 25 publications

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“…Chlorobium limicola forma thiosulfatophilum strain tassajara (kindly provided by N. Pfennig, Constance, Federal Republic of Germany) was grown, and membrane fragments were isolated as described previously (1). For oriented membrane multilayers, membrane fragments from C. limicola were separated from chlorosomes by the method of Schmidt (31).…”

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confidence: 99%

Diversity of Cytochrome bc Complexes: Example of the Rieske Protein in Green Sulfur Bacteria

1998

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The Rieske 2Fe2S cluster of Chlorobium limicola formathiosulfatophilum strain tassajara was studied by electron paramagnetic resonance spectroscopy. Two distinct orientations of its g tensor were observed in oriented samples corresponding to differing conformations of the protein. Only one of the two conformations persisted after treatment with 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone. A redox midpoint potential (Em ) of +160 mV in the pH range of 6 to 7.7 and a decreasing Em (−60 to −80 mV/pH unit) above pH 7.7 were found. The implications of the existence of differing conformational states of the Rieske protein, as well as of the shape of its Em -versus-pH curve, in green sulfur bacteria are discussed.

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Diversity of Cytochrome bc Complexes: Example of the Rieske Protein in Green Sulfur Bacteria

1998

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“…4). A previous study has shown that cytochromes c and b have two peaks between 550 nm and 560 nm, when absorption was measured at ultralow temperature [40]. It is likely that the plateau we observed in wild type is composed of two peaks of cytochromes c and b, but the peaks were not resolved at the room temperature we used for the measurement.The complement strain (C0531) and 015F07 had a wide peak similar to wild type with the maximum absorption at 558 nm and 556 nm, respectively.…”

Section: Resultsmentioning

confidence: 84%

“…Characteristic of the porphyrin compounds Soret band is the peak absorption at ~420 nm [39]. In addition, the wild type strain (8004) showed a peak plateau at absorption from 553.5 nm to 564 nm, while the mutant (0531pk) had only one peak at the absorption of 564 nm, which is typical of b-type cytochromes [40] (Fig. 4).…”

Section: Resultsmentioning

confidence: 99%

XC_0531 encodes a c-type cytochrome biogenesis protein and is required for pathogenesis in Xanthomonas campestris pv. campestris

et al. 2017

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BackgroundThe phytopathogenic Xanthomonas campestris pv.campestris is a gram-negative bacterium and the causal agent of black-rot disease of cruciferous crops. Many gram-negative bacteria possess a family of proteins, called Dsbs, which are involved in disulfide bond formation in certain periplasmic proteins. In our preliminary screening of the virulence to the plants we identified that gene XC_0531 which annotated gene dsbD of Xanthomonas campestris pv. campestris (Xcc) is related to the virulence to the host plants.ResultsHere, we found XC_0531 encoded a DsbD like protein. Its deletion is sensitive to DTT and copper, decreased accumulation of free thiols in periplasm. Its deletion also affected heme synthesis, position of Soret band and the production of peak c550. This suggests that XC_0531 is related to c-type cytochromes biogenesis. XC_0531 mutation decreased the utilization of different carbon sources (such as galactose, xylose, maltose, saccharose and glucose), reduced extracellular polysaccharide (EPS) production, decreased extracellular enzyme activities (protease, cellulose and amylase), slowed down growth rate of Xcc and weakened virulence to the plants. These results suggest that these phenotypes caused by XC_0531 mutation is possibly due to deficient biosynthesis of c-type cytochromes in respiration chain and the formation of disulfide bonds. Our work confirmed the function of XC_0531 and provide theory basis for scientists working on molecular mechanisms of cytochrome c biogenesis, pathogenesis of Xcc, development of EPS commercial values and protecting plant from black rot.ConclusionWe confirmed the function of gene XC_0531, which encodes a DsbD like protein, a protein correlated with c-type cytochrome biogenesis. This gene is related to the virulence to plants by affecting funtion of cytochromes c and probably disulfide bonds modification of proteins in type II secretion system (T2SS).Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-017-1056-9) contains supplementary material, which is available to authorized users.

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“…These halves are therefore tentatively referred to as ''N-c z '' and ''C-c z ,'' respectively. Other sequence data were obtained from the JGI microbial genomic database and the GenBank database b Photosynth Res (2010) 104: 189-199 193 resonance (ESR) spectroscopic method, but its function is still unknown (Albouy et al 1997).…”

Section: Ctepidum Cz-sol -F D F D a A K K L V D V R --C N K C H T L mentioning

confidence: 99%

C-type cytochromes in the photosynthetic electron transfer pathways in green sulfur bacteria and heliobacteria

et al. 2010

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Green sulfur bacteria and heliobacteria are strictly anaerobic phototrophs that have homodimeric type 1 reaction center complexes. Within these complexes, highly reducing substances are produced through an initial charge separation followed by electron transfer reactions driven by light energy absorption. In order to attain efficient energy conversion, it is important for the photooxidized reaction center to be rapidly rereduced. Green sulfur bacteria utilize reduced inorganic sulfur compounds (sulfide, thiosulfate, and/or sulfur) as electron sources for their anoxygenic photosynthetic growth. Membrane-bound and soluble cytochromes c play essential roles in the supply of electrons from sulfur oxidation pathways to the P840 reaction center. In the case of gram-positive heliobacteria, the photooxidized P800 reaction center is rereduced by cytochrome c-553 (PetJ) whose N-terminal cysteine residue is modified with fatty acid chains anchored to the cytoplasmic membrane.

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Membrane-Associated c-type Cytochromes from the Green Sulfur Bacterium Chlorobium limicola forma thiosulfatophilum: Purification and Characterization of Cytochrome c₅₅₃

Cited by 14 publications

References 25 publications

Diversity of Cytochrome bc Complexes: Example of the Rieske Protein in Green Sulfur Bacteria

Diversity of Cytochrome bc Complexes: Example of the Rieske Protein in Green Sulfur Bacteria

XC_0531 encodes a c-type cytochrome biogenesis protein and is required for pathogenesis in Xanthomonas campestris pv. campestris

C-type cytochromes in the photosynthetic electron transfer pathways in green sulfur bacteria and heliobacteria

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