The rate of entry of dioxygen and carbon monoxide into myoglobin.

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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Austin RH,Chan SS

doi

10.1016/S0006-3495(78)85354-5

subject

Has Abstract

pub_date

1978-10-01 00:00:00

pages

175-86

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(78)85354-5

journal_volume

24

pub_type

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