Here you can see a crystal structure of the Bovine Heart Cytochrome c Oxidase (PDB code: 9IKF)

Rendering by Francisco J. Enguita made with #ProteinImager

3dproteinimaging.com/protein-imag...

#SciArt #molecularart #cytochrome #oxidase #membrane #mitochondria #xray

Drs Ian Drobish & Hans Ackerman highlight Chandy John & colleagues’ @natmed.nature.com‬ article on elevating #UricAcid as an #antimalarial target. #Hyperuricemia #Malaria #Plasmodium #Xanthine #Oxidase @niaidnews.bsky.social‬ ‪@childrensnational.bsky.social

authors.elsevier.com/a/1l82h5Eb1x...

I am really happy to share our study about the 4-allylsyringol #oxidase from S. cavernae. It turned out to be a very interesting #flavoenzyme with high biocatalytic potential for 2,6-substituted phenols.

Kinetic and structural investigation of the 4-allyl syringol oxidase from Streptomyces cavernae 4-Phenol oxidases are proposed to be involved in the utilization of lignin-derived aromatic compounds. While enzymes with selectivity towards 4-hydrox…

The last research article of @danieleggerichs.bsky.social PhD thesis was just published, supported by wonderful collaboration with the @mattevilab.bsky.social it's part of a special collection for #flavins and #flavoproteins, and we report on a #flavin #oxidase
www.sciencedirect.com/science/arti...

Dehydrogenase versus Oxidase Function: The Interplay between Substrate Binding and Flavin Microenvironment Redox enzymes, mostly equipped with metal or organic cofactors, can vary their reactivity with oxygen by orders of magnitude. Understanding how oxygen reactivity is controlled by the protein milieu remains an open issue, with broad implications for mechanistic enzymology and enzyme design. Here, we address this problem by focusing on a widespread group of flavoenzymes that oxidize phenolic compounds derived from microbial lignin degradation, using either oxygen or cytochrome c as an electron acceptor. A comprehensive phylogenetic analysis revealed conserved amino acid motifs in the flavin-binding site. Using a combination of kinetic, mutagenesis, structural, and computational methods, we examined the role of these residues. Our results demonstrate that subtle and localized changes in the flavin environment can drastically impact oxygen reactivity. These effects are afforded through the creation or blockade of pathways for oxygen diffusion. Substrate binding plays a crucial role by potentially obstructing oxygen access to the flavin, thus influencing the enzyme’s reactivity. The switch between oxidase and dehydrogenase functionalities is thereby achieved through targeted, site-specific amino acid replacements that finely tune the microenvironment around the flavin. Our findings explain how very similar enzymes can exhibit distinct functional properties, operating as oxidases or dehydrogenases. They further provide valuable insights for the rational design and engineering of enzymes with tailored functions.

Great study on the question what defines an #oxidase vs. a #dehydrogenase... and vice versa #proteinengineering #biocatalysis #flavoprotein #flavin #enzymology

pubs.acs.org/doi/10.1021/...