Redox Properties of Protein Disulfide Bond in Oxidized Thioredoxin and Lysozyme:  A Pulse Radiolysis Study

We have studied the one-electron reduction of oxidized Chlamydomonas reinhardtii thioredoxin and compared it to that of hen egg white lysozyme, using CO2 •  - free radicals as reductants. This comparison shows that the thioredoxin disulfide/thiol redox couple has different properties than that of ly...

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Bibliographic Details

Published in:	Biochemistry (Easton) 2000-08, Vol.39 (31), p.9295-9301
Main Authors:	Lmoumène, C. El Hanine, Conte, D, Jacquot, J.-P, Houée-Levin, C
Format:	Article
Language:	eng
Subjects:	Alanine - genetics Amino Acid Substitution - genetics Animals Anions - chemistry Aspartic Acid - genetics Chickens Chlamydomonas reinhardtii - enzymology Chlamydomonas reinhardtii - genetics Disulfides - chemistry Electrons Free Radicals - chemistry Muramidase - chemistry Mutagenesis, Site-Directed Oxidation-Reduction Protons Pulse Radiolysis Sulfhydryl Compounds - chemistry Thioredoxins - chemistry Thioredoxins - genetics Tryptophan - genetics
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