Hydration-dependent conformational states of hemoglobin. Equilibrium and kinetic behavior.

Abstract

The equilibrium and kinetics of methemoglobin conversion to hemichrome induced by dehydration were investigated by visible absorption spectroscopy. Below about 0.20 g water per g hemoglobin only hemichrome was present in the sample; above this value, an increasing proportion of methemoglobin appeared with the increase in hydration. The transition between the two derivatives showed a time-dependent biphasic behavior and was observed to be reversible. The rates obtained for the transition of methemoglobin to hemichrome were 0.31 and 1.93 min-1 and for hemichrome to methemoglobin 0.05 and 0.47 min-1. We suggest that hemichrome is a reversible conformational state of hemoglobin and that the two rates observed for the transition between the two derivatives reflect the alpha- and beta-chains of hemoglobin.

• Authors: M F Colombo, R Sanches
• Journal: Biophysical chemistry (Biophys Chem) Vol. 36 Issue 1 Pg. 33-9 (May 1990) ISSN: 0301-4622 [Print] Netherlands
• PMID: 2207271 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Hemeproteins
• hemichrome
• Water
• Methemoglobin

Topics

• Desiccation
• Hemeproteins (chemistry)
• Humans
• Kinetics
• Methemoglobin (chemistry)
• Protein Conformation (drug effects)
• Spectrophotometry
• Water (pharmacology)