Results 61 to 70 of about 26,737 (217)
Aggregate, Volume 7, Issue 2, February 2026.A smart peptide hydrogel integrated with light‐responsive silver nanoclusters establishes a localized anaerobic niche, enabling hydrogenase function in oxygen‐rich biological environments. The system achieves sustained visible‐light‐driven H2 production, effectively scavenges reactive oxygen species, modulates immune responses, and significantly ...
Haishuo Ji +15 more
wiley +1 more source
MicrobiologyOpen, 2019 Acetaldehyde, a valuable commodity chemical, is a volatile inhibitory byproduct of aerobic fermentation in Zymomonas mobilis and in several other microorganisms.
Elina Balodite +6 more
doaj +1 more source
Protein Science, Volume 35, Issue 2, February 2026.Abstract Structural predictions have reached unprecedented accuracy. They leverage sequence‐specific data to capture all potential interactions a sequence has evolved to fulfill. AlphaFold derives information from three sources: learned parameters capturing intrinsic amino acid secondary structure and environment propensity; models of related proteins ...
Josep Triviño +14 more
wiley +1 more source
Proteins: Structure, Function, and Bioinformatics, Volume 94, Issue 2, Page 649-659, February 2026.ABSTRACT The sodium‐pumping ubiquinone oxidoreductase sodium pumping quinone reductase (NQR) is an important enzyme in the respiratory chain of multiple pathogenic gram‐negative bacteria. NQR has been proposed as a viable antibiotic target due to its importance in supporting energy‐consuming reactions and its absence in human cells.
Joseph. A. DePaolo‐Boisvert +3 more
wiley +1 more source
Environmental Microbiology Reports, Volume 18, Issue 1, February 2026.The oleic acid and azide inhibited the cytochrome c oxidase activity in Pseudomonas aeruginosa MCC 5300, shifting the electron flux towards bd‐oxidase. This resulted in more NADH consumption to maintain the proton gradient for energy generation. The rapid depletion of NADH triggered high mcl‐PHA accumulation.
Raghavendra Paduvari +1 more
wiley +1 more source
Protein quality control in the bacterial periplasm
Microbial Cell Factories, 2004 The proper functioning of extracytoplasmic proteins requires their export to, and productive folding in, the correct cellular compartment. All proteins in Escherichia coli are initially synthesized in the cytoplasm, then follow a pathway that depends ...
Betton Jean-Michel, Miot Marika
doaj +1 more source
Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials
Advanced Healthcare Materials, Volume 15, Issue 3, 19 January 2026.The production of recombinant proteins represents a fundamental step in the characterisation of marine invertebrate adhesives and in the development of bio‐inspired glues. The association of these proteins with other components such as ions, proteins, polysaccharides, or polymers enables the fabrication of biomaterials for various healthcare ...
Alessandra Whaite +4 more
wiley +1 more source
Flavin Biosynthesis Enhances Extracellular Electron Transfer in Bioengineered Escherichia coli
Advanced Science, Volume 13, Issue 2, 9 January 2026.Microbial electronics are promising for energy, sensing, environmental, and synthesis applications. E. coli are engineered with extracellular electron transfer (EET) pathways from a microbe that naturally produces current to enable bioelectronics based on E. coli.
Mohammed Mouhib +4 more
wiley +1 more source
Laccases from lactic acid bacteria show cuprous oxidase activity and capture Cu(II) and Ag(I) ions
Protein Science, Volume 35, Issue 1, January 2026.Abstract Several laccases derived from lactic acid bacteria (LAB) display specific structural features, such as two methionine residues at the entrance of the T1Cu center, and an extended C‐terminal end enriched in methionine and histidine. To investigate their functional roles, we engineered mutant variants of the laccase Pp4816 from Pediococcus ...
Raquel Gascó +6 more
wiley +1 more source
Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding
Protein Science, Volume 35, Issue 1, January 2026.Abstract Disulphide bonds (Dsbs) are essential for the folding, stability, and function of many secreted and membrane‐associated proteins in bacteria. In Gram‐negative species, these bonds are introduced by the Dsb enzyme family, with DsbA acting as the primary thiol oxidase.
Stephanie Penning +9 more
wiley +1 more source