-transparent.png){kind=logo}
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.
M F Colombo, and
R Sanches
September 1973,
The Journal of biological chemistry,
M F Colombo, and
R Sanches
June 2001,
Biochemistry,
M F Colombo, and
R Sanches
March 1997,
Biophysical journal,
M F Colombo, and
R Sanches
November 1985,
Biochemistry,
M F Colombo, and
R Sanches
March 1987,
Biochemistry,
M F Colombo, and
R Sanches
May 2014,
Biochemistry,
M F Colombo, and
R Sanches
November 2017,
Physical chemistry chemical physics : PCCP,
M F Colombo, and
R Sanches
January 2006,
Methods in enzymology,
M F Colombo, and
R Sanches
November 1986,
Biochemistry,
M F Colombo, and
R Sanches
August 2009,
Proceedings of the National Academy of Sciences of the United States of America,
