## Abstract The binding of azide ion to horseβheart 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
β¦ LIBER β¦
FTIR and EPR analysis of azide binding to horse heart myoglobin variants.
β Scribed by R. Bogumil; D.P. Hildebrand; E. Lloyd; C.M. Overall; H.-L. Tang; M. Smith; A.G. Mauk
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 81 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0162-0134
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The binding mode of azide to the ferric form of Aplysia limacina myoglobin has been studied by X-ray crystallography. The three-dimensional structure of the complex has been refined at 1.9 A resolution to a crystallographic R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to t