Abstract
Mitochondrial cytochromec (horse), which is a very efficient electron donor to bacterial photosynthetic reaction centersin vitro, binds to the reaction center ofRhodospirillum rubrum with an approximate dissociation constant of 0.3–0.5 µM at pH 8.2 and low ionic strength. The binding site for the reaction center is on the frontside of cytochromec which is the side with the exposed heme edge, as revealed by differential chemical acetylation of lysines of free and reaction-center-bound cytochromec. In contrast, bacterial cytochromec 2 was found previously to bind to the detergent-solubilized reaction center through its backside, i.e., the side opposite to the heme cleft [Rieder, R., Wiemken, V., Bachofen, R., and Bosshard, H. R. (1985).Biochem. Biophys. Res. Commun. 128, 120–126]. Binding of mitochondrial cytochromec but not of mitochondrial cytochromec 2 is strongly inhibited by low concentrations of poly-l-lysine. The results are difficult to reconcile with the existence of an electron transfer site on the backside of cytochromec 2.
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References
Bosshard, H. R. (1979).Methods Biochem. Anal. 25, 273–301.
Bosshard, H. R., Davidson, M. W., Knaff, D. B., and Millett, F. (1986).J. Biol. Chem. 261, 190–193.
Brautigan, D. L., Ferguson-Miller, S., and Margoliash, E. (1978).Meth. Enzymol. 53, 128–164.
Dickerson, R. E., and Timkovich, R. (1975). InThe Enzymes (Boyer, P. D. ed.), Vol. 11, Academic Press, New York, pp. 397–547.
Dixon, H. B. F. (1976).Biochem. J. 159, 161–162.
Ferguson-Miller, S., Brautigan, D. L., and Margoliash, E. (1978).J. Biol. Chem. 253, 149–159.
Margoliash, E., and Bosshard, H. R. (1983).Trends Biochem. Sci. 8, 316–320.
Nicholls, P. (1974).Biochim. Biophys. Acta 346, 261–310.
Rickle, G. K., and Cusanovich, M. A. (1979).Arch. Biochem. Biophys. 197, 589–598.
Rieder, R., and Bosshard, H. R. (1980).J. Biol. Chem. 255, 4732–4739.
Rieder, R., Wiemken, V., Bachofen, R., and Bosshard, H. R. (1985).Biochem. Biophys. Res. Commun. 128, 120–126.
Rosen, D., Okamura, M. Y., and Feher, G. (1980).Biochemistry 19, 5687–5692.
Salemme, F. R. (1977).Annu. Rev. Biochem. 46, 299–329.
Schleifer, A., and Willis, B. G. (1980).Hewlett-Packard J. 31, 11–17.
Smith, H. T., Staudenmeyer, N., and Millett, F. (1977).Biochemistry 16, 4971–4974.
Snozzi, M., and Bachofen, R. (1979).Biochim. Biophys. Acta 546, 236–247.
Sponholtz, D. K., Brautigan, D. L., Loach, P. A., and Margoliash, E. (1976).Anal. Biochem. 72, 255–260.
Takano, T., and Dickerson, R. E. (1980).Proc. Natl. Acad. Sci. USA 77, 6371–6375.
Weber, P. C., and Tollin, G. (1985).J. Biol. Chem. 260, 5568–5573.
van der Waal, H., and van Grondelle, R. (1985).13th Int. Congr. Biochem., Amsterdam, Abstract MO-518.
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Bosshard, H.R., Snozzi, M. & Bachofen, R. Interaction of horse cytochromec with the photosynthetic reaction center ofRhodospirillum rubrum . J Bioenerg Biomembr 19, 375–382 (1987). https://doi.org/10.1007/BF00768540
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DOI: https://doi.org/10.1007/BF00768540