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Author Title Year Publication Serial Volume (down) Pages
Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements 1989 Biochimica et Biophysica Acta 3803 996 49-56
Saigo, S. Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c 1981 Biochimica et Biophysica Acta 3871 669 13-20
Hasumi, H. Kinetic studies on isomerization of ferricytochrome c in alkaline and acid pH ranges by the circular dichroism stopped-flow method 1980 Biochimica et Biophysica Acta 3876 626 265-276
Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W. Folding units govern the cytochrome c alkaline transition 2003 Journal of Molecular Biology 3781 331 37-43
Hirota, S.; Suzuki, M.; Watanabe, Y. Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c 2004 Biochemical and Biophysical Research Communications 3777 314 452-458
Pierce, M.M.; Nall, B.T. Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization 2000 Journal of Molecular Biology 3853 298 955-969
Dyson, H.J.; Beattie, J.K. Spin state and unfolding equilibria of ferricytochrome c in acidic solutions 1982 The Journal of Biological Chemistry 3807 257 2267-2273
Nicol, C.J.; Davidson, H.P.D.; Harris, P.A.; Waters, A.J.; Wilson, A.D. Study of crib-biting and gastric inflammation and ulceration in young horses 2002 The Veterinary record 83 151 658-662
Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique 2001 Journal of the American Chemical Society 3788 123 6649-6653
Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase 1981 European Journal of Biochemistry / FEBS 3810 113 425-433