Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex.

The first crystal structure of a ternary redox protein complex was comprised of the enzyme methylamine dehydrogenase (MADH) and two electron transfer proteins, amicyanin and cytochrome c-551i from Paracoccus denitrificans [Chen et al. Science 1994, 264, 86-90]. The arrangement of the proteins suggested possible electron transfer from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron, although the distance between the metals is large.

Nicotine determination in mushrooms by LC-MS/MS with preliminary studies on the impact of drying on nicotine formation.

A problem concerning significant amounts of nicotine in dried wild mushrooms (mainly Boletus edulis from China) has been reported to the European Commission. As a consequence, the European Food Safety Authority (EFSA) proposed temporary maximum residue levels (MRLs) of 0.036 mg kg(-1) for fresh wild mushrooms and 1.

Search for a more adequate test to predict the long-term migration from the PVC gaskets of metal lids into oily foods in glass jars.

As shown previously, the conventional testing procedure for simulating long-term migration from the gaskets of metal closures into oily foods does not adequately reflect reality. It appears to be impossible to accelerate migration to the extent that the situation at the end of the shelf life of a product can be anticipated in a few days or weeks. Therefore, we investigated whether long-term migration could be extrapolated from migration rates determined for new lids.

Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus.

Methylamine can be used as the sole carbon source of certain methylotrophic bacteria. Methylamine dehydrogenase catalyzes the conversion of methylamine into formaldehyde and donates electrons to the electron transfer protein amicyanin. The crystal structure of the complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus has been determined, and the rate of electron transfer from the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase to the copper ion of amicyanin in solution has been determined.