Amicyanin and Complexes of Amicyanin with Methylamine Dehydrogenase and Cytochrome c551i
F Scott Mathews
Washington University School of Medicine, St. Louis, MO, USA
Search for more papers by this authorF Scott Mathews
Washington University School of Medicine, St. Louis, MO, USA
Search for more papers by this authorAbstract
Amicyanin is the key component of a soluble periplasmic electron transfer chain in the bacterium Paracoccus denitrificans that passes electrons from an amine substrate to a terminal oxidase in the periplasmic membrane. It directly and specifically transfers electrons from methylamine dehydrogenase (MADH) to an inducible c-type cytochrome, c551i. Amicyanin is a 12.5-kDa monomeric cupredoxin, MADH is a 124-kDa heterotetramer oxidizing enzyme, and c551i is a 17.5-kDa monomeric cytochrome. Crystal structures of amicyanin, a binary MADH–amicyanin complex and a ternary MADH–amicyanin–cytochrome c551i complex, are described and correlated with their kinetic and electron transfer properties in solution.
3D Structure
Ribbon diagram of AMI viewed down the central axis of the β-sandwich. The colors of the nine β-strands progress from strand 1 on the left in blue to strand 9 at the upper right in red. The four ligands to the copper atom in the upper right are also shown. This diagram was made with MOLSCRIPT21 and RASTER3D.22 PDB code: 1AAC
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