Direct Measurement of the Reduction Potential of Catalytically Active Cytochrome c Peroxidase Compound I: Voltammetric Detection of a Reversible, Cooperative Two-Electron Transfer Reaction
Author:
Affiliation:
1. Inorganic Chemistry Laboratory, Oxford University South Parks Road, Oxford OX1 3QR, U.K.
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja952489f
Reference19 articles.
1. Bosshard, H. R.; Anni, H.; Yonetani, T. InPeroxidases in Chemistry and Biology,Vol.II; Everse, J., Everse, K. E., Grisham, M. B., Eds.; CRC Press: Boca Raton, FL, 1990; pp 51−84. Poulos, T.; Fenna, R. InMetal Ions in Biological Systems,Vol.30, Sigel, H., Sigel, A., Eds.; Marcel Dekker Inc. New York, 1994; pp 25−75.
2. Cytochrome c peroxidase binds two molecules of cytochrome c: Evidence for a low-affinity, electron-transfer-active site on cytochrome c peroxidase
3. Identification by ENDOR of Trp 191 as the Free-Radical Site in Cytochrome c Peroxidase Compound ES
4. Modification of the F0 portion of ECF1-F0 by the water-soluble carbodiimide EDC and effect on the proton channeling function
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