Abstract：
:In aqueous glycerol solutions, the rate constant for the formation of compound I of horseradish peroxidase from hydrogen peroxide is independent of the viscosity. However, whem m-chloroperbenzoic acid is used to form compound I, the rate is viscosity dependent, indicating that this reaction is diffusion controlled. The problems in obtaining accurate information about diffusion-controlled reactions are discussed as is the possible significance of diffusion control. Ethanol has been used in previous studies to decrease the dielectric constant of the medium but it was found that its dominant effect on horseradish peroxidase was to bind to the sixth coordination position of the heme ion. The stability of the native enzyme in different environments was tested by difference absorption and circular dichroic spectroscopy and new circular dichroic data for compound I are reported.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Dunford HB,Hewson WDdoi
10.1021/bi00632a023subject
Has Abstractpub_date
1977-06-28 00:00:00pages
2949-57issue
13eissn
0006-2960issn
1520-4995journal_volume
16pub_type
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