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- Page, Taylor
R.; Hoffman, Brian M.
- Biochemistry 2015 v.54 no.5 pp. 1188-1197
- crystal structure; cytochrome c; cytochrome-c peroxidase; dissociation; electron transfer; mutation; nuclear magnetic resonance spectroscopy; thermodynamics; yeasts
- ... Extensive studies of the physiological protein–protein electron-transfer (ET) complex between yeast cytochrome c peroxidase (CcP) and cytochrome c (Cc) have left unresolved questions about how formation and dissociation of binary and ternary complexes influence ET. We probe this issue through a study of the photocycle of ET between Zn-protoporphyrin IX-substituted CcP(W191F) (ZnPCcP) and Cc. Photo ...
- PubMed Central:
- Baas, Bert-Jan; Poddar, Harshwardhan; Geertsema, Edzard
M.; Rozeboom, Henriette J.; de Vries, Marcel P.; Permentier, Hjalmar
P.; Thunnissen, Andy-Mark W.H.; Poelarends, Gerrit J.
- Biochemistry 2015 v.54 no.5 pp. 1219-1232
- crystal structure; decarboxylation; dehalogenation; hydroxybenzaldehyde; oxalic acid; oxidation; oxygen; oxygenases; sequence homology; stable isotopes
- ... The vast majority of characterized oxygenases use bound cofactors to activate molecular oxygen to carry out oxidation chemistry. Here, we show that an enzyme of unknown activity, RhCC from Rhodococcus jostii RHA1, functions as an oxygenase, using 4-hydroxyphenylenolpyruvate as a substrate. This unique and complex reaction yields 3-hydroxy-3-(4-hydroxyphenyl)-pyruvate, 4-hydroxybenzaldehyde, and ox ...