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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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 253; no. 1; pp. 238 - 241
Main Authors Ho, K, Klapper, M H, Dorfman, L M
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 10.01.1978
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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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)38294-7