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Plants, humans and hemoglobins.
Suman Kundu1, James T Trent, Mark S Hargrove
1Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
Trends in Plant Science
|August 21, 2003
Summary
Hexacoordinate hemoglobins, found in plants and animals, regulate oxygen differently than myoglobin. These proteins may share a common physiological role, especially during hypoxic stress.
Area of Science:
- Biochemistry
- Molecular Biology
- Physiology
Background:
- Hemoglobin structure and function understanding is evolving.
- Leghemoglobins utilize unique heme pocket amino acids to regulate oxygen affinity, differing from myoglobin.
- Hexacoordinate hemoglobins, initially identified in plants, are now recognized across diverse species.
Purpose of the Study:
- To re-evaluate hemoglobin structure and function in light of new developments.
- To explore the distinct oxygen-binding mechanisms of leghemoglobins.
- To investigate the potential common physiological function of hexacoordinate hemoglobins in plants and animals.
Main Methods:
- Comparative analysis of hemoglobin structures.
- Investigation of heme pocket amino acid variations.
- Examination of protein expression patterns under hypoxic conditions.
Main Results:
- Leghemoglobins exhibit a novel mechanism for oxygen affinity regulation.
- Hexacoordinate hemoglobins are characterized by intramolecular ligand coordination.
- These proteins are upregulated in plants and animals during hypoxia.
Conclusions:
- Hexacoordinate hemoglobins possess a unique structural and functional profile.
- A shared physiological role for hexacoordinate hemoglobins in plants and animals is plausible, particularly under stress.