Semi-synthetic analogs of cytochrome Substitutions for methionine at position 80
| Autor: | Ashok K. Koul, Paul K. Warme, Paul T. Nix, Gail Folena Wasserman |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Hemeprotein
biology Ethionine Cytochrome c peroxidase Cytochrome b Stereochemistry Cytochrome c Cytochrome P450 reductase Cytochrome c Group Succinates Heme Biochemistry Genetics and Molecular Biology (miscellaneous) Structure-Activity Relationship chemistry.chemical_compound Methionine chemistry Coenzyme Q – cytochrome c reductase biology.protein Cytochrome c oxidase Cyanogen Bromide Cysteine Oxidoreductases |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure. 623:457-460 |
| ISSN: | 0005-2795 |
| DOI: | 10.1016/0005-2795(80)90275-5 |
| Popis: | Derivatives of cytochrome c having S- methyl cysteine and ethionine substituted for methionine residue 80 have been synthesized in order to study the effects of structural perturbations near the heme on the biological function of cytochrome c . The ethionine derivative has 96% as much activity as native cytochrome c in the succinate oxidase system, whereas the S- methyl cysteine analog is totally inactive. |
| Databáze: | OpenAIRE |
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