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Molecular basis for redox‐Bohr and cooperative effects in cytochrome c 3 from Desulfovibrio desulfuricans ATCC 27774: Crystallographic and modeling studies of oxidized and reduced high‐resolution structures at pH 7.6
Author(s) -
Bento Isabel,
Matias Pedro M.,
Baptista António M.,
da Costa Patricia N.,
van Dongen Walter M.A.M.,
Saraiva Lígia M.,
Schneider Thomas R.,
Soares Cláudio M.,
Carrondo Maria A.
Publication year - 2003
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10431
Subject(s) - chemistry , redox , desulfovibrio , cytochrome , electron transfer , crystallography , cooperativity , bohr effect , heme , protonation , hydrogenase , cytochrome c , propionate , stereochemistry , electron transport chain , photochemistry , inorganic chemistry , sulfate , hydrogen , biochemistry , hemoglobin , organic chemistry , ion , mitochondrion , oxygen–haemoglobin dissociation curve , enzyme
The tetraheme cytochrome c 3 is a small metalloprotein with ca. 13,000 Da found in sulfate‐reducing bacteria, which is believed to act as a partner of hydrogenase. The three‐dimensional structure of the oxidized and reduced forms of cytochrome c 3 from Desulfovibrio desulfuricans ATCC 27774 at pH 7.6 were determined using high‐resolution X‐ray crystallography and were compared with the previously determined oxidized form at pH 4.0. Theoretical calculations were performed with both structures, using continuum electrostatic calculations and Monte Carlo sampling of protonation and redox states, in order to understand the molecular basis of the redox‐Bohr and cooperativity effects related to the coupled transfer of electrons and protons. We were able to identify groups that showed redox‐linked conformational changes. In particular, Glu61, His76, and propionate D of heme II showed important contributions to the redox‐cooperativity, whereas His76, propionate A of heme I, and propionate D of heme IV were the key residues for the redox‐Bohr effect. Upon reduction, an important movement of the backbone region surrounding hemes I and II was also identified, that, together with a few redox‐linked conformational changes in side‐chain residues, results in a significant decrease in the solvent accessibility of hemes I and II. Proteins 2004. © 2003 Wiley‐Liss, Inc.

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