Analysis of the kinetics of electron transfer reactions of hemoglobin and myoglobin with inorganic complexes. |
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Authors: | A G Mauk H B Gray |
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Institution: | Arthur Amos Noyes Laboratory of Chemical Physics California Institute of Technology Pasadena, California 91125 USA |
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Abstract: | The kinetics of methemoglobin reduction by Fe(EDTA)2? have been studied and found to follow a second order rate law with k = 29.0 ?1 s?1 25°C, μ = 0.2 , pH 7.0 (phosphate)], , and . The electrostatics-corrected self-exchange rate constant (k11corr) for hemoglobin based on the Fe(EDTA)2? cross-reaction is 2.79×10?3?1 s?1. This rate constant is compared with others reported for a water-soluble iron porphyrin and calculated from published data for the reactions of myoglobin and hemoglobin with Fe(EDTA)2? and Fe(CDTA)2?/?. The k11corr values for these systems range over ten orders of magnitude with heme ? myoglobin > hemoglobin. |
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Keywords: | To whom correspondence should be directed |
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