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The crystal structure of the iron‐free cytochrome c peroxidase and its implication for the enzymatic mechanism
Author(s) -
Su Xiao-Dong,
Yonetani Takashi,
Skoglund Ulf
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00910-4
Subject(s) - chemistry , histidine , heme , peroxidase , electron transfer , cytochrome c peroxidase , fluorescence , myoglobin , cytochrome c , active center , enzyme , stereochemistry , crystallography , biochemistry , photochemistry , mitochondrion , physics , quantum mechanics
We report the refined structure of an iron‐free form of cytochrome c peroxidase (CcP) at 2.3 Å resolution. The backbone comparison between native CcP and iron‐free CcP shows that the two structures have the same protein fold within experimental error. The only difference noted is in the heme pocket where the distance between the proximal histidine and the center of the protoporphyrin has increased. The results show that the iron‐free CcP should be a good substitute for native CcP in fluorescence studies and thus also validate previous studies using iron‐free CcPs as efficient fluorescent probes in electron transfer studies.