Fractionation and partial characterization of the heme active site of lactoperoxidase
β Scribed by T.D. Rae; H.M. Goff
- Book ID
- 103570395
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 48 KB
- Volume
- 59
- Category
- Article
- ISSN
- 0162-0134
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π SIMILAR VOLUMES
The multifunctional nature of proteins that have iron-heme cofactors with noncovalent histidine linkage to the protein is controlled by the heme environment. Previous studies of these active-site structures show that the primary difference is the length of the iron-proximal histidine bond, which can
Hemoglobin (Hb) from Chelidonichthys kumu was studied by resonance Raman and electronic absorption spectroscopy in the iron(III) and iron(II) states and in the presence of and CO at various pH values. All forms showed O 2 the appearance of two m(CxC) stretching modes around 1620 and 1630 cm-1 in con