Interaction of the chlorite-based drug WF10 and chlorite with hemoglobin, methemoglobin and ferryl hemoglobin

Interaction of the chlorite-based drug WF10 and chlorite with hemoglobin, methemoglobin and... The interaction of the chlorite-based drug solution WF10 with human oxyhemoglobin and oxidized hemoglobin forms was investigated monitoring the corresponding spectral changes in heme states. The chlorite component of WF10 converts oxyhemoglobin into methemoglobin with a rate of 35.4 M−1s−1. Methemoglobin is also formed upon the interaction of ferryl hemoglobin and WF10/chlorite. The rate of this interconversion depends on the oxidation state of ferryl hemoglobin. This rate is 114 M−1s−1, when ferryl hemoglobin was generated upon reaction of oxyhemoglobin and hydrogen peroxide. A considerable higher rate (6600 M−1s−1) is measured between the chlorite components of WF10 and ferryl hemoglobin after formation of the latter species from methemoglobin. WF10/chlorite inactivates also methemoglobin as evidenced by the continuous decrease of the Soret band and all other absorbances with a rate of 8.3 M−1s−1. In all interconversions, the chlorite component of WF10 was the active principle as shown in experiments applying pure chlorite at the same concentration as in WF10. Thus, WF10 is able to diminish efficiently the yield of cytotoxic hemoglobin species that might appear after excessive hemolysis of red blood cells under pathologic situations. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Biochemistry and Biophysics Elsevier

Interaction of the chlorite-based drug WF10 and chlorite with hemoglobin, methemoglobin and ferryl hemoglobin

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Publisher
Elsevier
Copyright
Copyright © 2015 Elsevier Inc.
ISSN
0003-9861
eISSN
1096-0384
D.O.I.
10.1016/j.abb.2015.09.009
Publisher site
See Article on Publisher Site

Abstract

The interaction of the chlorite-based drug solution WF10 with human oxyhemoglobin and oxidized hemoglobin forms was investigated monitoring the corresponding spectral changes in heme states. The chlorite component of WF10 converts oxyhemoglobin into methemoglobin with a rate of 35.4 M−1s−1. Methemoglobin is also formed upon the interaction of ferryl hemoglobin and WF10/chlorite. The rate of this interconversion depends on the oxidation state of ferryl hemoglobin. This rate is 114 M−1s−1, when ferryl hemoglobin was generated upon reaction of oxyhemoglobin and hydrogen peroxide. A considerable higher rate (6600 M−1s−1) is measured between the chlorite components of WF10 and ferryl hemoglobin after formation of the latter species from methemoglobin. WF10/chlorite inactivates also methemoglobin as evidenced by the continuous decrease of the Soret band and all other absorbances with a rate of 8.3 M−1s−1. In all interconversions, the chlorite component of WF10 was the active principle as shown in experiments applying pure chlorite at the same concentration as in WF10. Thus, WF10 is able to diminish efficiently the yield of cytotoxic hemoglobin species that might appear after excessive hemolysis of red blood cells under pathologic situations.

Journal

Archives of Biochemistry and BiophysicsElsevier

Published: Nov 1, 2015

References

  • Biochemistry
    Hofbauer, S.; Gruber, C.; Pirker, K.; Sündermann, A.; Schaffner, I.; Jakopitsch, C.; Oostenbrink, C.; Furtmüller, P.G.; Obinger, C.
  • Biochemistry
    Nagababu, E.; Ramasamy, S.; Rifkind, J.M.; Jia, Y.; Alayash, A.I.

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