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Volume Changes in Binding of Ligands to Methemoglobin and Metmyoglobin

✍ Scribed by Gabriel B. Ogunmola, Walter Kauzmann and Adam Zipp

Book ID
123654057
Publisher
National Academy of Sciences
Year
1976
Tongue
English
Weight
495 KB
Volume
73
Category
Article
ISSN
0027-8424

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Spin contribution to the thermodynamics
Spin contribution to the thermodynamics of ligand binding to methemoglobins and metmyoglobins. I. Azide ion binding to horse-heart myoglobin
✍ A. C. I. Anusiem; M. Kelleher πŸ“‚ Article πŸ“… 1978 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 446 KB πŸ‘ 2 views

## Abstract The binding of azide ion to horse‐heart myoglobins has been studied at pH 6.98 and at various temperatures. The results show that the azide complex is not completely loe spin and that the spin population is strongly dependent on temperature. We have shown that with some assumption it is