Structural studies of Desulfovibrio vulgaris ferrocytochrome c3 by two-dimensional NMR.
Two-dimensional NMR has been used to make specific assignments for the four haems in Desulfovibrio vulgaris (Hildenborough) ferrocytochrome c3 and to determine their haem core architecture. The NMR signals from the haem protons were assigned according to type using two-dimensional NMR experiments which led to four sets of signals, one for each of the haems. Specific assignments were obtained by calculating the ring current shifts which arise from other haems and aromatic residues. Observation of interhaem NOEs confirmed the assignments and established that the relative orientation of the haems is identical to that found in the crystal structure of D. vulgaris (Miyazaki F.) ferricytochrome c3. Assignments were also made for all the aromatic residues except for the haem ligands and F20, which is shifted under the main envelope of signals. The NOEs observed between these aromatic protons and haem protons confirm the similarity between the structures in solution and in the crystal. The assignments reported here are the basis for the cross-assignments of the four microscopic haem redox potentials to specific haems in the protein structure [Salgueiro, C. A., Turner, D. L., Santos, H., LeGall, J. and Xavier, A. V. (1992) FEBS Lett., in the press]
Turner
D L
DL
Department of Chemistry, University of Southampton, England.
Salgueiro
C A
CA
LeGall
J
J
Xavier
A V
AV
D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry*; D016969:Desulfovibrio vulgaris / Q000378:metabolism*; D006418:Heme / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation
D003574:Cytochrome c Group; D006418:Heme; C017165:cytochrome c(3)