Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species.

@article{Smagghe2006SlowLB,
  title={Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species.},
  author={Benoit J. Smagghe and Gautam Sarath and Emily J. H. Ross and Jean-Louis Hilbert and Mark S Hargrove},
  journal={Biochemistry},
  year={2006},
  volume={45 2},
  pages={
          561-70
        }
}
Hexacoordinate hemoglobins are found in many living organisms ranging from prokaryotes to plants and animals. They are named "hexacoordinate" because of reversible coordination of the heme iron by a histidine side chain located in the heme pocket. This endogenous coordination competes with exogenous ligand binding and causes multiphasic relaxation time courses following rapid mixing or flash photolysis experiments. Previous rapid mixing studies have assumed a steady-state relationship between… CONTINUE READING
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A model for ligand binding to hexacoordinate hemoglobins, Biochemistry

J. T. Trent, III, A. N. Hvitved, M. S. Hargrove
2001
View 3 Excerpts
Highly Influenced

Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes.

Proceedings of the National Academy of Sciences of the United States of America • 2005

Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination

D. de Sanctis, S. Dewilde, +5 authors M. Bolognesi
J. Mol. Biol • 2004