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Fast folding kinetics and stabilization of apo‐cytochrome c
Author(s) -
Borgia Alessandro,
Gianni Stefano,
Brunori Maurizio,
Travaglini-Allocatelli Carlo
Publication year - 2008
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/j.febslet.2008.02.046
Subject(s) - heme , chemistry , folding (dsp implementation) , kinetics , cytochrome c , protein folding , hemeprotein , fluorescence , cytochrome , stereochemistry , biophysics , biochemistry , crystallography , biology , mitochondrion , enzyme , physics , quantum mechanics , electrical engineering , engineering
It is generally accepted that in the c ‐type cytochromes the covalently bound heme plays a primary role in the acquisition of the folded state. Here, we show that a stabilized site‐directed variant of apo‐cyt c 551 from Pseudomonas aeruginosa ( Pa ‐apocyt F7A/W77F) retains native‐like features in the presence of sodium sulfate even in the absence of heme. By time‐resolved intrinsic fluorescence, we have evidence that Pa ‐apocyt F7A/W77F may acquire a compact, native‐like conformation within microseconds. These results challenge current thinking about the role of the heme group in the folding of c ‐type cytochromes.