A macromolecular transducer as illustrated by trout hemoglobin IV.
- 1 September 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (9), 4310-4312
- https://doi.org/10.1073/pnas.75.9.4310
Abstract
Oxygen binding by trout Hb IV was investigated as a function of pH up to 10 atm (1 MPa) of pure O2. An extreme proteon-oxygen linkage, which gives rise to a Root effect was revealed. The results are discussed in relation to the function of the Hb as an oxygen pump. The system is of special interest as providing a prototype of a macromolecule acting as a transducer by coupling 2 allosterically linked reactions.Keywords
This publication has 9 references indexed in Scilit:
- Spectral changes and allosteric transition in trout haemoglobinNature, 1975
- Molecular Adaptation to Physiological Requirements: The Hemoglobin System of TroutCurrent Topics in Cellular Regulation, 1975
- An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriersBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- The Effect of pH on the Reactions of Oxygen and Carbon Monoxide with the Hemoglobin of the Carp, Cyprinus carpioJournal of Biological Chemistry, 1970
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Physiology of the swimbladder.Physiological Reviews, 1966
- METABOLIC STUDIES ON THE GAS GLAND OF THE SWIM BLADDERThe Biological Bulletin, 1955
- SECRETION OF GASES AGAINST HIGH PRESSURES IN THE SWIMBLADDER OF DEEP SEA FISHES I. OXYGEN DISSOCIATION IN BLOODThe Biological Bulletin, 1954
- THE RESPIRATORY FUNCTION OF THE BLOOD OF MARINE FISHESThe Biological Bulletin, 1931