The location of redox centers in biological membranes determined by resonance x-ray diffraction. II. Analysis of the resonance diffraction data.
In the preceding paper (Stamatoff, J., Eisenberger, P., Blasie, J.K., Pachence, J.M., Tavormina, A., Erecinska, M., Dutton P.L. and Brown, G. (1982) Biochim. Biophys. Acta 679, 177-187), we described the observation of resonance X-ray scattering effects from intrinsic metal atoms associated with redox centers in membrane proteins on the lamellar X-ray diffraction from oriented multilayers of reconstituted membranes. In this paper, we discuss the possible methods of analysis of such data and present the results of our model refinement analysis concerning (a) the location of the cytochrome c heme iron atom in the profile structure of a reconstituted membrane containing a photosynthetic reaction center-cytochrome c complex and (b) the location of the heme a and a3 iron atoms in the profile structure of a reconstituted membrane containing cytochrome oxidase. The former results are of special importance because they provide a test of the validity of the resonance diffraction data and the methods of analysis, since the location of cytochrome c in the reaction center-cytochrome c membrane profile is known independently of the resonance diffraction experiments.
D000818:Animals; D002462:Cell Membrane; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003574:Cytochrome c Group; D003576:Electron Transport Complex IV; D006736:Horses; D010084:Oxidation-Reduction; D014961:X-Ray Diffraction
D003574:Cytochrome c Group; D003576:Electron Transport Complex IV