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Literature summary for 1.4.9.1 extracted from

  • de la Lande, A.; Babcock, N.S.; Rezac, J.; Sanders, B.C.; Salahub, D.R.
    Surface residues dynamically organize water bridges to enhance electron transfer between proteins (2010), Proc. Natl. Acad. Sci. USA, 107, 11799-11804.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Organism UniProt Comment Textmining
Paracoccus denitrificans
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