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A denaturation-induced proton-uptake study of horse ferricytochrome c.
Biochem J. 1989 Mar 1;258(2):595-8. doi: 10.1042/bj2580595.
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Ionization of the heme propionate substituents in pseudomonad cytochromes c-551.
FEBS Lett. 1992 Oct 26;311(3):213-6. doi: 10.1016/0014-5793(92)81105-u.
8
Chemical modification of the haem propionate of cytochrome c.
Biochem J. 1980 Jan 1;185(1):47-57. doi: 10.1042/bj1850047.
9
Involvement of lysines-72 and -79 in the alkaline isomerization of horse heart ferricytochrome c.
Biochemistry. 1980 Mar 18;19(6):1117-20. doi: 10.1021/bi00547a012.
10
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
Proc Natl Acad Sci U S A. 1974 Jul;71(7):2892-4. doi: 10.1073/pnas.71.7.2892.

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Ionization of tyrosine and lysine residues in native and modified horse cytochrome c.
Biochem J. 1983 Sep 1;213(3):679-86. doi: 10.1042/bj2130679.
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Electron transfer in biology. The function of cytochrome c.
Faraday Discuss Chem Soc. 1982;74:311-29. doi: 10.1039/dc9827400311.
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Structural role of the tyrosine residues of cytochrome c.
Biochem J. 1982 Jul 1;205(1):153-65. doi: 10.1042/bj2050153.
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Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C.
Biochem Biophys Res Commun. 1971 Dec 3;45(5):1134-43. doi: 10.1016/0006-291x(71)90137-9.
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Infrared titration of lysozyme carboxyls.
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Some properties of the 695 millimicron band of Pseudomonas cytochrome C.
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