The rate of entry of dioxygen and carbon monoxide into myoglobin

R. H. Austin, S. S. Chan

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

The model for carbon monoxide or dioxygen recombination with heme proteins developed by the group at the University of Illinois is reexamined. We propose that the carbon monoxide or dioxygen molecule enters the protein at essentially a diffusion-limited rate determined by the solvent viscosity and that the protein offers no important barriers to this entry. The viscosity dependence of the entry rate k(ED), its magnitude (1 x 10(10) M(-1)s(-1), and the rate of quenching of triplet states of protoprophyrin IX in apomyoglobin by dioxygen are used as supporting evidence. Comparison is made to the model of a fluctuating protein developed by G. Weber.

Original languageEnglish (US)
Pages (from-to)175-186
Number of pages12
JournalBiophysical Journal
Volume24
Issue number1
DOIs
StatePublished - 1978

All Science Journal Classification (ASJC) codes

  • Biophysics

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