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A general exit strategy of monoheme cytochromes c and c 2 in electron transfer complexes?
Author(s) -
De March Matteo,
Brancatelli Giovanna,
Demitri Nicola,
De Zorzi Rita,
Hickey Neal,
Geremia Silvano
Publication year - 2015
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1410
Subject(s) - electron transfer , redox , cytochrome c , chemistry , electron transport chain , crystallography , photosynthetic reaction centre , peroxidase , stereochemistry , photochemistry , mitochondrion , biochemistry , inorganic chemistry , enzyme
Using our previously reported maps of the electrostatic surface of horse heart ferri‐ and ferro‐cyt c , comparisons were made between the complementary electrostatic surfaces of three cyt c peroxidase–cyt c complexes and the photosynthetic reaction center–cyt c complex, considering both iron oxidation states. The results obtained were consistent with a sliding mechanism for the electron shuttle on the surface of the protein complexes, promoted by the change in iron oxidation state. This mechanism was found to be in agreement with theoretical and NMR studies reported in the literature. Importantly, the analysis also provided a rationale for recognition of nonproductive associations. As we have previously reported the same conclusion on examination of redox partners of cyt c in the mitochondrial respiratory pathway, our hypothesis is that the proposed mechanism could represent a general exit strategy of monoheme cyts c and c 2 in electron transfer complexes. © 2015 IUBMB Life, 67(9):694–700, 2015