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Extra info for Biomembranes Part N: Transport in Bacteria, Mitochondria, and Chloroplasts: Protonmotive Force
Hunter, and J. C. Bennett, Anal. Biochem. 103, 184 (1980). 51 L. E. Henderson, S. Oroszlan, and W. Konigsberg, Anal. Biochem. 93, 153 (1979). 52 C. Barnabeu, F. P. Conde, and D. Vazquez, Anal. Biochem. 84, 97 (1978). 44 ELECTRON TRANSFER  TABLE III DIFFERENT N-TERMINAL AMINO ACID SEQUENCES OF BOVINE AND PIG HEART AND LIVER CYTOCHROME-C OXIDASE SUBUNITS Subunit Source N-terminal sequence Via Bovine heart Bovine liver Ala-Ser-Ala-Ala-Lys-Gly-Asp-His Ser-Ser-Glv-Ala-His-Gly-Glu-Glu VIIa Bovine heart Bovine liver Phe-Glu-Asn-Arg-Val-AlaPhe-Glu-Asn-Lvs-Val-Ala- Pig heart Pig liver Phe- ?
Henderson, S. Oroszlan, and W. Konigsberg, Anal. Biochem. 93, 153 (1979). 52 C. Barnabeu, F. P. Conde, and D. Vazquez, Anal. Biochem. 84, 97 (1978). 44 ELECTRON TRANSFER  TABLE III DIFFERENT N-TERMINAL AMINO ACID SEQUENCES OF BOVINE AND PIG HEART AND LIVER CYTOCHROME-C OXIDASE SUBUNITS Subunit Source N-terminal sequence Via Bovine heart Bovine liver Ala-Ser-Ala-Ala-Lys-Gly-Asp-His Ser-Ser-Glv-Ala-His-Gly-Glu-Glu VIIa Bovine heart Bovine liver Phe-Glu-Asn-Arg-Val-AlaPhe-Glu-Asn-Lvs-Val-Ala- Pig heart Pig liver Phe- ?
5 nm gives the artifactual absorbance change (B) due to dilution of the Phenol Red. 5 of size (A + B). If there is any deviation from this, then the pH of the cytochrome c solution must be adjusted until the step change has the predicted magnitude. Cytochrome c is itself strongly charged, and thus the possibility arises that the protons appearing extravesicularly on addition of cytochrome c may be released from the vesicle surface owing to a differential interaction with the oxidized and reduced cytochrome ~9(though this would have to be uncoupler sensitive; see above).
Biomembranes Part N: Transport in Bacteria, Mitochondria, and Chloroplasts: Protonmotive Force by Nathan P. Colowick, Nathan P. Kaplan, Sidney Fleischer, Becca Fleischer