1I77

CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ESSEX 6

Summary for 1I77

• Entry DOI: 10.2210/pdb1i77/pdb
• Descriptor: CYTOCHROME C3, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: multi-heme cytochrome c, electron transport
• Biological source: Desulfovibrio desulfuricans
• Total number of polymer chains: 1
• Total formula weight: 14103.43

Authors

Einsle, O.,Foerster, S.,Mann, K.H.,Fritz, G.,Messerschmidt, A.,Kroneck, P.M.H. (deposition date: 2001-03-08, release date: 2001-08-29, Last modification date: 2024-11-13)

Primary citation

Einsle, O.,Foerster, S.,Mann, K.,Fritz, G.,Messerschmidt, A.,Kroneck, P.M.
Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6.
Eur.J.Biochem., 268:3028-3035, 2001

PubMed Abstract: Cytochrome c3, 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 c3 were obtained and X-ray diffraction data were collected to below 2 A resolution. The structure was solved by molecular replacement using cytochrome c3 from D. desulfuricans ATCC 27774 as a search model.

PubMed: 11358521
DOI: 10.1046/j.1432-1327.2001.02195.x

Experimental method

X-RAY DIFFRACTION (1.95 Å)