Figure 1.
Figure 1: The nitrite reductase dimer. A front view with the
dimer axis orientated vertically, the five haems in each monomer
(white), the Ca^2+ ions (grey) and Lys 133 which coordinates the
active-site iron atom (yellow). In the right monomer, the
protein chain is coloured blue from the amino-terminal end to
red at the carboxy-terminal end, in the left monomer according
to secondary structure. The dimer interface is dominated by
three long -helices
per monomer. All haems in the dimer are covalently attached to
the protein and their iron atoms are arranged almost in a plane
parallel to the plane of the paper.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1999,
400,
476-480)
copyright 1999.
-helices
per monomer. All haems in the dimer are covalently attached to
the protein and their iron atoms are arranged almost in a plane
parallel to the plane of the paper.