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Cytb1-1-Ascorbate metabolism in plants: physiological function and biochemical properties of cytochrome b561

ABSTRACT: What is the physiological function of cytochrome b561 in Arabidopsis thaliana - We want to check which possible changes occur in gene expression by knocking out the AtCytb1 gene. au08-01_cytb561 - cytb1-1 Keywords: gene knock out

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE19739 | GEO | 2010/04/01

SECONDARY ACCESSION(S): PRJNA122203

REPOSITORIES: GEO

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Cytb1-1-Ascorbate metabolism in plants: physiological function and biochemical properties of cytochrome b561

Project description:What is the physiological function of cytochrome b561 in Arabidopsis thaliana - We want to check which possible changes occur in gene expression by knocking out the AtCytb1 gene. au08-01_cytb561 - cytb1-1 Keywords: gene knock out 4 dye-swap - CATMA arrays

2010-03-31 | E-GEOD-19739 | biostudies-arrayexpress

ccme-The cytochrome pathway and cytochrome C biogenesis

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Transcriptional response of Mycobacterium tuberculosis to inhibition of Cytochrome bd oxidase and Cytochrome bcc:aa3 oxidase

Project description:Comparative analysis of the transcriptional response, as quantified by RNA-Seq, of Mycobacterium tuberculosis (Mtb) during inhibition of the terminal cytochrome oxidases, Cytochrome bd oxidase and Cytochrome bcc:aa3. This study was designed to evaluate the efficacy if a novel small molecule inhibitor of the Cytochrome bd oxidase. Specifically, we compared the transcriptional response of Mtb during inhibition by Q203 with a Cytochrome bd deletion mutant to the transcriptional response of Mtb treated with a combination of Q203 and the purported Cytorchomre bd small molecule inhibitor (ND-011992).

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The unusual properties of the photosynthetic cytochrome c550 from the red algal lineage evidence additional biological roles

Project description:Cytochrome c550 is an extrinsic component in the luminal side of photosystem II in cyanobacteria, as well as in eukaryotic algae from the red photosynthetic lineage including, among others, diatoms. By using strong and specific protease inhibitors we have confirmed that cytochrome c550 from the diatom Phaeodactylum tricornutum is expressed as a truncated form lacking the last hydrophobic residues at the C-terminal.. Phaeodactylum tricornutum cytochrome c550 seems to be modified at a post-translational level as the gene is appropriately transcribed. In addition, co-immunoprecipitation and mass spectrometry experiments have allowed the identification of novel interactions of Phaeodactylum tricornutum cytochrome c550 with proteins related to the CO2 concentrating mechanism and assimilation located in the chloroplast pyrenoid. Furthermore, immunoelectron microscopy analysis indicates that although cytochrome c550 is mainly located in the thylakoid domain of the chloroplast, it can also be found in the pyrenoid. The results are interpreted in terms of a specific protein modification associated to a higher PSII turnover or to new alternative functions of the heme protein, maybe related to carbon fixation.

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Engineering ascorbate peroxidase activity into cytochrome c peroxidase.

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Evidence for a key role of cytochrome bo3 oxidase in respiratory energy metabolism of Gluconobacter oxydans

Project description:The obligatory aerobic acetic acid bacterium Gluconobacter oxydans oxidizes a variety of substrates in the periplasm by membrane-bound dehydrogenases, which transfer the reducing equivalents to ubiquinone. Two quinol oxidases, cytochrome bo3 and cytochrome bd, then catalyze transfer of the electrons from ubiquinol to molecular oxygen. In this study, mutants lacking either of these terminal oxidases were characterized. Deletion of the cydAB genes for cytochrome bd had no obvious influence on growth, whereas the lack of the cyoBACD genes for cytochrome bo3 severely reduced the growth rate and the cell yield. Using a respiration activity monitoring system and adjusting different levels of oxygen availability, hints for a low oxygen affinity of cytochrome bd oxidase were obtained, which were supported by measurements of oxygen consumption in a respirometer. The H+/O ratio of the ΔcyoBACD mutant with mannitol as substrate was 0.56 ± 0.11 and more than 50% lower than that of the reference strain (1.26 ± 0.06) and the delta-cydAB mutant (1.31 ± 0.16), indicating that cytochrome bo3 oxidase is the main component for proton extrusion via the respiratory chain. Plasmid-based overexpression of cyoBACD led to increased growth rates and growth yields, both in the wild type and the delta-cyoBACD mutant, suggesting that cytochrome bo3 might be the rate-limiting factor of the respiratory chain.

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