Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.
To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to...
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Autores principales: | , , , , , , , , , , , |
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Formato: | article |
Lenguaje: | EN |
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Public Library of Science (PLoS)
2011
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Acceso en línea: | https://doaj.org/article/c3757a2a4ad44e8c9c0077fd8210a03c |
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