Crystallization (Comment) | Organism |
---|---|
molecular dynamics simulations of the complex of redox proteins methylamine dehydrogenase and amicyanin to generate configurations over a duration of 40 ns in conjunction with an electron trnasfer pathway analysis. In the wild-type complex, the most frequently occurring molecular configurations afford superior electronic coupling due to the consistent presence of a water molecule hydrogen-bonded between the donor and acceptor sites. The water bridge function of nearby solvent-organizing residues by limiting the exchange of water molecules between the sterically constrained electron transfer region and the more turbulent surrounding bulk. When the water bridge is affected by a mutation, bulk solvent molecules disrupt it, resulting in reduced electronic coupling | Paracoccus denitrificans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus denitrificans | - |
- |
- |