Abstract
Heme cross-linking of membrane cytochromes as a structural principle: cytochrome b-559, b 6 , and cytochrome oxidase. After the Mr 9,000 protein of cyt b–559 was purified and its NH2-terminus sequenced (1), its psbE gene and the downstream psbF gene located and sequenced on the spinach chloroplast genome (2), an intermolecular heme cross-linked dimeric structure of cytochrome b–559 was proven by the findings that (a) each polypeptide contains only one histidine (2), (b) the psbE and psbF gene products are present in the purified protein in a 1:1 stoichiometry (3), and (c) the heme coordination is bis-histidine (Fig. la; ref. 4). Thus, a dimer would be required to provide two His residues for heme coordination. There are several reasons, including the 1:1 stoichiometry, for believing that the heme-binding unit is an α-β heterodimer (5), but this has not been rigorously proven.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Widger, W.R., Cramer, W.A., Hermodson, M., Meyer, D., and Gullifor, M. (1984) J. Biol. Chem 259, 3870–3876
Herrmann, R.G., Alt, J., Schiller, B., Widger, W.R., and Cramer, W.A. (1984) FEBS Lett. 176, 239–244
Widger, W.R., Cramer, W.A., Hermodson, M., and Herrmann, R.G. (1985) FEBS Lett. 191, 186–190
Babcock, G.T., Widger, W.R., Cramer, W.A., Oertling, W.A., and Metz, J.G. (1985) Biochemistry 24, 3638–3644
Cramer, W.A., Theg, S.M., and Widger, W.R. (1986) Photosyn. Res. 10, 393–403
Widger, W.R., Cramer, W.A., Herrmann, R.G., and Trebst, A. (1984) Proc. Natl. Acad. Sci. 81, 674–678
Saraste, M. (1984) FEBS Lett. 166, 367–372
Davidson, E. and Daldal, F. (1987) J. Mol. Biol. 195, 13–24
Kallas, T., Spiller, S., and Malkin, R. (1988) J. Biol. Chem. 263, 14334–14342
Hauska, G., Nitschke, W., and Herrmann, R.G. (1988) J. Bioenerg. Biomem. 20, 211–228
Shiver, J.W., Peterson, A.A., Widger, W.R., Furbacher, P.N., and Cramer, W.A. (1989) Meth. Enzymol. 172, 439–461, Academic Press, Orlando
Holm, L., Saraste, M., and Wikström, M.K.F. (1987) EMBO J. 6, 2819–2823
Tae, G.-S., Black, M.T., Cramer, W.A., Vallon, O., and Bogorad, L. (1988) Biochemistry 27, 9075–9080
Åkerlund, H.E. and Andersson, B. (1983) Biochim. Biophys. Acta 725, 34–40
Sayre, R.T., Andersson, B., and Bogorad, L. (1986) Cell 47, 601–608
Vallon, O, Tae, G.-S., Cramer, W.A., Simpson, D., Hoyer-Hansen, G., and Bogorad, L. (1989) Biochim. Biophys. Acta 975, 132–141
Ortiz, W. and Malkin, R. (1985) Biochim. Biophys. Acta 808, 164–170
Markwell, M.K. and Fox, C.F. (1978) Biochemistry 17, 4809–4817
Boyd, D., Manoil, C., and Beckwith, J. (1987) Proc. Natl. Acad. Sci. 84, 8525–8529
diRago, J.-P. and Colson, A.M. (1988) J. Biol. Chem. 263, 12564–12570
diRago, J.-P., Coppee, J.-Y., and Colson, A.M. (1989) J. Biol. Chem. 264, in press
Howell, N. and Gilbert, K. (1988) J. Mol. Biol. 203, 607–618
Daldal, F. (1987) in Cytochrome Systems: Molecular Biology and Bioenergetics (Papa, S., et al., eds.), pp. 23–34, Plenum Press, New York
Dekker, J.P., Bowlby, N.R., and Yocum, CF. (1989) FEBS Lett., in press
Miyazaki, A., Shina, T., Toyoshima, Y., Gounaris, K., and Barber, J. (1989) Biochim. Biophys. Acta 975, 142–147
Whitmarsh, J. and Cramer, W.A. (1978) Biochim. Biophys. Acta 501, 83–93
Larsson, C., Jansson, C., Ljungberg, U., Akerlund, H.E., and Andersson, B. (1984) in Adv. Photosyn. Res, I., (Sybesma, C., ed.), pp. 363–366
Horton, P., Whitmarsh, J., and Cramer, W.A. (1976) Arch. Biochem. Biophys. 176, 519–524
Innes, J.B., and Brudvig, G. (1989) Biochemistry 28, 1116–1125
Thompson, L.K. and Brudvig, G. (1988) Biochemistry 27, 6653–6658
Gounaris, K., Chapman, D.J., and Barber, J. (1988) FEBS Lett. 234, 374–378
Bricker, T.M., Odon, W.R., and Quierolo, L.B. (1988) FEBS Lett. 231, 111–117
Doyle, M.P., Li, L.B., Yu, L., and Yu, C-A. (1989) J. Biol. Chem 264, 1387–1392
Crofts, A., et al. (1987) in Cytochrome Systems: Molecular Biology and Bioenergetics (Papa, S., et al., eds.), pp. 617–624, Plenum Press, NY.
Khorana, H.G. (1988) J. Biol.Chem 263, 7439–7442
Cramer, W.A., Black, M.T., Widger, W.R., and Girvin, M.E. (1987) in The Light Reactions (Barber, J., ed.), pp. 447–493, Elsevier, Amsterdam
Szczepaniak, A. and Cramer, W.A. (1989) these Proceedings and submitted for publication
Szczepaniak, A., Black, M.T., and Cramer, W.A. (1989) Zeit, für Naturforsch. 44c, 453–461
Willey, D.L., Auffret, A.D., and Gray, J.C. (1984) Cell 36, 555–562
Yeates, T.O., Komiya, H., Rees, D.C., Allen, J.P., and Feher, G. (1987) Proc. Natl. Acad Sci., U.S.A. 84, 6438–6442
Graan, T. and Ort, D.R. (1983) J. Biol. Chem 258, 2381–2386
Crofts, A.R. (1985) in The Enzymes of Biological Membranes (Martinosi, A., ed.), IV, pp. 347–382, Plenum, New York
Joliot, P. and Delosme, R. (1974) Biochim. Biophys. Acta 357, 267–284
Velthuys, B.R. (1979) Proc. Natl. Acad. Sci., U.S.A. 76, 2765–2769
Joliot, P. and Joliot, A. (1986) Biochim. Biophys. Acta 849, 211–222
Moss, D.A. and Rich, P.R. (1987) Biochim. Biophys. Acta 894, 189–197
Hangarter, R.P., Jones, R.W., Ort, D.R., and Whitmarsh, H. (1987) Biochim. Biophys. Acta 890, 106–115
Rich, P.R. (1988) Biochim. Biophys. Acta 932, 33–42
Bouges-Bocquet, B. (1981) Biochim. Biophys. Acta 635, 327–340
Hope, A.B. and Mathews, D.B. (1987) Aust. J. Pl. Physiol. 14, 29–46
Rich, P.R. and Moss, D.A. (1987) in The Light Reactions (Barber, J., ed.), pp. 421–445, Elsevier, Amsterdam
Hurt, E.C., Hauska, G., and Shahak, Y. (1982) FEBS Lett. 149, 211–216
Willms, I., Malkin, R., and Chain, R.K. (1988) Arch. Biochem. Biophys. 263, 36–44
Selak, M. and Whitmarsh, J. (1982) FEBS Lett 150, 286–292
Girvin, M.E. and Cramer, W.A. (1984) Biochim. Biophys. Acta 767, 29–38
Jones, R.W. and Whitmarsh, J. (1988) Biochim. Biophys. Acta 933, 319–333
Furbacher, P.N., Girvin, M.E., and Cramer, W.A. (1989) these Proceedings and Biochemistry 28, in press
Hladik, J., Snozzi, M., and Bachofen, R. (1987) Biochem. Biophys. Res. Comm. 148, 170–177
Clark, R.D. and Hind, G. (1983) Proc. Natl. Acad. Sci. 80, 6249–6253
Von Jagow, G. and Link, T.A. (1986) Meth. Enzymol. 126, 253–
Hope, A.R. and Rich, P.R. (1989) Biochim. Biophys. Acta 975, 96–103
Davies, E.C. and Bendall, D.S. (1987) in Prog. Photosyn. Res. (Biggins, J., ed.), 2, 2185–2188
Wikström, M.K.F. and Saraste, M. (1984) in Bioenergetics (Ernster, L., ed.), pp. 49–94, Elsevier, Amsterdam
Moss, D.A. and Bendall, D.S. (1984) Biochim. Biophys. Acta 767, 389–395
O’Keefe, D.P. (1983) FEBS Lett. 162, 349–354
Gounaris, K., Sandby, C., Andersson, B., and Barber, J. (1983) FEBS Lett. 156, 170–174
Koudelka, A.P., Kambadur, N., Bradley, D.K., and Ferguson, K.A. (1983) Biochim. Biophys. Acta 751, 121–126
Browse, J., Kunst, L., Anderson, S., Hugly, S., and Somerville, C. (1989) Plant Physiol. 90, 522–529
McKeon, T.A. and Stumpf, P.K. (1982) J. Biol. Chem. 257, 12141–12147
Constantopoulos, G. and Bloch, K. (1967) J. Biol. Chem. 242, 3538–3542
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Springer Science+Business Media New York
About this chapter
Cite this chapter
Cramer, W.A., Furbacher, P.N., Szczepaniak, A., Tae, GS. (1990). The Chloroplast b Cytochromes: Crosslinks, Topography, and Functions. In: Baltscheffsky, M. (eds) Current Research in Photosynthesis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0511-5_489
Download citation
DOI: https://doi.org/10.1007/978-94-009-0511-5_489
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6716-4
Online ISBN: 978-94-009-0511-5
eBook Packages: Springer Book Archive