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• W1998460935 startingPage "309" @default.
• W1998460935 abstract "The crystal structure of erythrocruorin has been refined by constrained crystallographic refinement at 1·4 Å resolution in the following ligand states: aquomet (Fe3+, high spin), cyanomet (Fe3+, low spin), deoxy (Fe2+, high spin) and carbonmonoxy (Fe2+, low spin). The final R-value at this resolution is better than 0·19 for each of these models. The positional errors of the co-ordinates are less than 0·1 Å. The root-mean-square differences between the deoxygenated and the ligated erythrocruorin are about 0·1 Å, being largest for cyanomet-erythrocruorin. The changes in tertiary structures propagate from the location of primary events and often fade out at the molecular surface. Helix E passing the distal side of the haem group is affected most by the direct contact with the ligand bound to the haem iron. Steric hindrance by the distal residue IleE11 forces the cyanide and carbonmonoxide ligands to bind at an angle to the haem axis. The strain at the ligand is partially relieved by movement of the haem deeper into the haem pocket and rearrangement of neighbouring residues. The differences in iron location with respect to the mean haem plane are spin-dependent but unexpectedly small (the largest value is 0·15 Å between deoxy and carbonmonoxy-erythrocruorin). Spin state changes seem to have little influence on the porphyrin stereochemistry; it is determined primarily by the chemical properties of the ligand and its interaction with the haem and the globin. These non-covalent interactions are largely responsible for the initiation of the structural changes on ligand binding." @default.
• W1998460935 created "2016-06-24" @default.
• W1998460935 creator A5022368910 @default.
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• W1998460935 date "1979-01-01" @default.
• W1998460935 modified "2023-10-03" @default.
• W1998460935 title "Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution" @default.
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• W1998460935 doi "https://doi.org/10.1016/0022-2836(79)90332-2" @default.
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