Oxidoreductases are key enzymes in biocatalysis, but their dependence on the cofactor nicotinamide adenine dinucleotide (phosphate) (NAD(P)) presents challenges due to its high consumption and ...

Once the cofactor is added, the enzyme becomes the active “holoenzyme”. Cofactors can either be ions, such as zinc and iron ions, or organic molecules, such as vitamins or vitamin-derived ...

Finally, enzymes of the sulphite oxidase family contain haem cofactors. Recently, another link between the metabolic pathways of molybdenum and iron was discovered. In plants (and most probably ...

Natural hydrogen-producing enzymes are large and extremely sensitive to oxygen. This makes it difficult to use them for the applied production of green hydrogen. Researchers from the ...

Some enzymes cannot function unless they attach to a specific non-protein molecule, known as cofactors. There are two types of cofactors, ions and coenzymes. Ions are inorganic molecules that ...

“The cofactor specificity is mainly engineered in the glucose dehydrogenase because that’s the enzyme that charges the cofactor with electrons,” Li says. NMN + made a particularly good ...

Enzymes are often held in this appropriate conformation by small molecules called cofactors. I am fond of cofactors. I appreciate how, despite their structural simplicity, these helper molecules play ...

Little is currently known about the molecular determinants of energy barriers along enzyme catalytic pathways ... dual role for this ubiquitous cofactor. By using a combination of biophysical ...

"Although several enzymes are known to contain a quinone cofactor derived from a tryptophan residue, the mechanism involved in post-translational modification, as well as the structures of the ...

Researchers have identified how such a cofactor, the so-called hydrogen cluster, is assembled. Specifically, they describe the previously unexplained role of the enzyme HydF, which is involved in ...