The riboflavin-sensitized photooxidation of horseradish apoperoxidase

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dc.contributor.authorSilva, E.
dc.contributor.authorBarrera, M.
dc.date.accessioned2019-12-28T02:45:27Z
dc.date.available2019-12-28T02:45:27Z
dc.date.issued1985
dc.description.abstractNative horseradish peroxidase, as well as its reduced and carboxymethylated form, and the apoenzyme, showed resistance to photodynamic action. Sensitivity to this action was detected only in reduced and carboxymethylated apoenzyme, when the photooxidation of its histidine residues was observed. When analyzing the bulk hydrophobic character (Hf) and the accessibility coefficients (Br) in those amino acid residues which can be subjected to photooxidation in horseradish peroxidase, it was found that all of them are situated in hydrophobic zones with low accessibility coefficients. This could justify the high resistance of this enzyme to photodynamic action. The only exception is tryptophan-117, which has low values of Hf and Br, and therefore its resistance to photodynamic action can only be explained in terms of its location and environment. Tryptophan-117 would be situated in a zone of antiparallel?-structure, according to Chou and Fasman's predictive method for protein conformation.
dc.fuente.origenSpringer
dc.identifier.doi10.1007/BF01212653
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/27124
dc.identifier.urihttp://link.springer.com/article/10.1007/BF01212653
dc.issue.numeroNo. 1
dc.language.isoen
dc.revistaRadiation and Environmental Biophysicses_ES
dc.subject.ddc570
dc.subject.deweyBiologíaes_ES
dc.subject.otherAminoácidoses_ES
dc.subject.otherPeroxidasases_ES
dc.subject.otherHistidinaes_ES
dc.subject.otherBiofísicaes_ES
dc.titleThe riboflavin-sensitized photooxidation of horseradish apoperoxidasees_ES
dc.typeartículo
dc.volumenVol. 24
sipa.codpersvinculados68719
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