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Last modified: 9 September 1998

Bibliography on structural studies of soluble cytochrome b562

  1. Barker, P.D. and Freund, S.M.V. (1996) Bis­methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme­ligand interactions. Biochemistry 35, 13627-13635.
  2. Barker, P.D., Nerou, E.P., Freund, S.M.V. and Fearnley, I.M. (1995) Conversion of cytochrome b562 to c­type cytochromes. Biochemistry 34, 15191-15203.
  3. Barker, P.D., Nerou, E.P., Cheesman, M.R., Thomson, A.J., de Oliveira, P. and Hill, H.A.O. (1996) Bis­methionine ligation to heme iron in mutants of cytochrome b562. 1. Spectroscopic and electrochemical characterization of the electronic properties. Biochemistry 35, 13618-13626.
  4. Bullock, P.A. and Myer, Y.P. (1978) Circular dichroism and resonance Raman studies of cytochrome b562 from Escherichia coli. Biochemistry 17, 3084-3091.
  5. Czerwinski, E.W. and Mathews, F.S. (1974) Location of the iron atom and the non­crystallographic symmetry elements in cytochrome b562. J. Mol. Biol. 86, 49-57.
  6. Feng, Y.Q. and Sligar, S.G. (1991) Effect of heme binding on the structure and stability of Escherichia coli apocytochrome b562. Biochemistry 30, 10150-10155.
  7. Feng, Y.Q., Wand, A.J. and Sligar, S.G. (1991) 1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562. Biochemistry 30, 7711-7717.
  8. Feng, Y.Q., Sligar, S.G. and Wand, A.J. (1994) Solution structure of apocytochrome b562. Nature Struct. Biol. 1, 30-35.
  9. Fuentes, E.J. and Wand, A.J. (1998a) Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange. Biochemistry 37, 3687-3698.
  10. Fuentes, E.J. and Wand, A.J. (1998b) Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37, 9877-9883.
  11. Hamada, K., Bethge, P.H. and Mathews, F.S. (1995) Refined structure of cytochrome b562 from Escherichia coli at 1.4 Å resolution. J. Mol. Biol. 247, 947-962.
  12. Ishida, Y., Konishi, K., Aida, T. and Nagamune, T. (1998) Apocytochrome b562 as a novel chiral host molecule: The first enantioselective reconstitution. Chem. Eur. J. 4, 1148-1153.
  13. Lederer, F., Glatigny, A., Bethge, P.H., Bellamy, H.D. and Mathews, F.S. (1981) Improvement of the 2.5 Å resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics. J. Mol. Biol. 148, 427-448.
  14. Mathews, F.S., Bethge, P.H. and Czerwinski, E.W. (1979) The structure of cytochrome b562 from Escherichia coli at 2.5 Å resolution. J. Biol. Chem. 254, 1699-1706.
  15. Myer, Y.P. and Bullock, P.A. (1978) Cytochrome b562 from Escherichia coli: conformational, configurational, and spin­state characterization. Biochemistry 17, 3723-3729.
  16. Robinson, C.R., Liu, Y., Thomson, J.A., Sturtevant, J.M. and Sligar, S.G. (1997) Energetics of heme binding to native and denatured states of cytochrome b562. Biochemistry 36, 16141-16146.
  17. Weber, P.C., Salemme, F.R., Mathews, F.S. and Bethge, P.H. (1981) On the evolutionary relationship of the 4­alpha­helical heme proteins. The comparison of cytochrome b562 and cytochrome c'. J. Biol. Chem. 256, 7702-7704.
  18. Wilkinson, K.W., Ford, G.C., Moir, A.J., Rice, D.W., Rodgers, H.F., Smith, J.M.A., Stillman, T.J., and Goward, C.R. (1997) Crystallization of cytochrome b562 from Erwinia chrysanthemi. Acta Crystallogr. D53, 197-199.
  19. Wittung­Stafshede, P., Gray, H.B. and Winkler, J.R. (1997) Rapid formation of a four­helix bundle. Cytochrome b562 folding triggered by electron transfer. J. Am. Chem. Soc. 119, 9562-9563.
  20. Wu, J.Z., La Mar, G.N., Yu, L.P., Lee, K.B., Walker, F.A., Chiu, M.L. and Sligar, S.G. (1991) 1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: Evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation. Biochemistry 30, 2156-2165.
  21. Xavier, A.V., Czerwinski, E.W., Bethge, P.H. and Mathews, F.S. (1978) Identification of the haem ligands of cytochrome b562 by X­ray and NMR methods. Nature 275, 245-247.