Kinetics of carbon monoxide binding to singly reduced human methemoglobin
The kinetics of reaction of singly reduced methemoglobin (HbFe3(3+)Fe2+) with carbon monoxide have been investigated by the pulse radiolysis method. The rate constant for carbon monoxide binding to this form of hemoglobin is 4.1 X 10(6) M-1 S-1 at 24 degrees in our solutions. This value compares wit...
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Published in | The Journal of biological chemistry Vol. 253; no. 1; pp. 238 - 241 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
10.01.1978
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Subjects | |
Online Access | Get full text |
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Summary: | The kinetics of reaction of singly reduced methemoglobin (HbFe3(3+)Fe2+) with carbon monoxide have been investigated by the
pulse radiolysis method. The rate constant for carbon monoxide binding to this form of hemoglobin is 4.1 X 10(6) M-1 S-1 at
24 degrees in our solutions. This value compares with existing values for various forms of hemoglobin ranging from 4 X 10(6)
to 6.5 X 10(6) M-1 S-1. Addition of inositol hexaphosphate to the solutions results in a lower rate constant for carbon monoxide
binding amounting to 1.1 X 10(5) M-1 S-1. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(17)38294-7 |