Dynamics of carbon monoxide binding by heme proteins

R. H. Austin, K. Beeson, L. Eisenstein, H. Frauenfelder, I. C. Gunsalus, V. P. Marshall

Research output: Contribution to journalArticle

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Abstract

Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50°K for myoglobin and 25°K for cytochrome P-450 in glycerol-water solution. Above 240°K the reaction is second order; between 240° and 200°K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150°K the reaction follows a power law and is approximately 103 times faster for cytochrome P-450 than for myoglobin.

Original languageEnglish (US)
Pages (from-to)541-543
Number of pages3
JournalScience
Volume181
Issue number4099
DOIs
StatePublished - Jan 1 1973
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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    Austin, R. H., Beeson, K., Eisenstein, L., Frauenfelder, H., Gunsalus, I. C., & Marshall, V. P. (1973). Dynamics of carbon monoxide binding by heme proteins. Science, 181(4099), 541-543. https://doi.org/10.1126/science.181.4099.541