A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer.

ABSTRACT: The joint x-ray/neutron diffraction model of the Type I copper protein, amicyanin from Paracoccus denitrificans was determined at 1.8 A resolution. The protein was crystallized using reagents prepared in D(2)O. About 86% of the amide hydrogen atoms are either partially or fully exchanged, which correlates well with the atomic depth of the amide nitrogen atom and the secondary structure type, but with notable exceptions. Each of the four residues that provide copper ligands is partially deuterated. The model reveals the dynamic nature of the protein, especially around the copper-binding site. A detailed analysis of the presence of deuterated water molecules near the exchange sites indicates that amide hydrogen exchange is primarily due to the flexibility of the protein. Analysis of the elec

SUBMITTER: Sukumar N 

PROVIDER: S-EPMC2872398 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature