Publications by authors named "A Atteia"

Sequential membrane filtration of water samples is commonly used to monitor the diversity of aquatic microbial eukaryotes. This capture method is efficient to focus on specific taxonomic groups within a size fraction, but it is time-consuming. Centrifugation, often used to collect microorganisms from pure culture, could be seen as an alternative to capture microbial eukaryotic communities from environmental samples.

View Article and Find Full Text PDF

Volatile fatty acids found in effluents of the dark fermentation of biowastes can be used for mixotrophic growth of microalgae, improving productivity and reducing the cost of the feedstock. Microalgae can use the acetate in the effluents very well, but butyrate is poorly assimilated and can inhibit growth above 1 gC.L.

View Article and Find Full Text PDF

The study shows the biochemical and enzymatic divergence between the two aldehyde-alcohol dehydrogenases of the alga Polytomella sp., shedding light on novel aspects of the enzyme evolution amid unicellular eukaryotes. Aldehyde-alcohol dehydrogenases (ADHEs) are large metalloenzymes that typically perform the two-step reduction of acetyl-CoA into ethanol.

View Article and Find Full Text PDF
Article Synopsis
  • Hybrid cluster proteins (HCPs) are metalloproteins containing an iron-sulfur-oxygen cluster, found in all life forms but primarily studied in certain anaerobic parasites and photosynthetic microalgae, notably Chlamydomonas reinhardtii, which has four HCP genes.
  • Research indicates that HCPs in C. reinhardtii likely originated from a single alpha proteobacterial gene and expanded through duplication, with studies on HCP1 and HCP3 revealing their unique redox properties and structures.
  • Experiments show that both nitrate and darkness significantly increase HCP levels in C. reinhardtii under oxygen-rich conditions, suggesting a connection between HCPs and
View Article and Find Full Text PDF

Aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes, where their physiological role and regulation are, however, largely unknown. Herein we provide the first molecular and enzymatic characterization of the ADHE from the photosynthetic microalga Purified recombinant ADHE catalyzed the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde, and ethanol but seemed to be poised toward the production of ethanol from acetaldehyde.

View Article and Find Full Text PDF