Open AccessSpectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c 3 from Desulfovibrio desulfuricans Essex 6
Author(s) -
Einsle Oliver,
Foerster Stefanie,
Mann Karlheinz,
Fritz Günter,
Messerschmidt Albrecht,
Kroneck Peter M. H.
Publication year - 2001
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2001.02195.x
Subject(s) - periplasmic space , cytochrome c , cytochrome , chemistry , hydrogenase , electron paramagnetic resonance , crystallography , stereochemistry , biochemistry , physics , nuclear magnetic resonance , enzyme , mitochondrion , escherichia coli , gene
Cytochrome c 3 , a small (14‐kDa) soluble tetraheme protein was isolated from the periplasmic fraction of Desulfovibrio desulfuricans strain Essex 6. Its major physiological function appears to be that of an electron carrier for the periplasmic hydrogenase. It has been also shown to interact with the high‐molecular‐mass cytochrome complex in the cytoplasmic membrane, which eventually feeds electrons into the membraneous quinone pool, as well as with the membrane‐associated dissimilatory sulfite reductase. The EPR spectra show features of four different low‐spin Fe(III) hemes. Orthorhombic crystals of cytochrome c 3 were obtained and X‐ray diffraction data were collected to below 2 Å resolution. The structure was solved by molecular replacement using cytochrome c 3 from D. desulfuricans ATCC 27774 as a search model.