Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6.
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.
Einsle
O
O
Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany.
Foerster
S
S
Mann
K
K
Fritz
G
G
Messerschmidt
A
A
Kroneck
P M
PM
D000595:Amino Acid Sequence; D016227:Benzoquinones / Q000737:chemistry; D002455:Cell Division; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D003901:Desulfovibrio / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D004583:Electrons; D006418:Heme / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019897:Periplasm / Q000737:chemistry; D011485:Protein Binding; D020539:Sequence Analysis, Protein; D013053:Spectrophotometry; D014466:Ultraviolet Rays; D014961:X-Ray Diffraction
D016227:Benzoquinones; D003574:Cytochrome c Group; C004532:quinone; D006418:Heme; C017165:cytochrome c(3)