De Simone G, Di Masi A, Sbardella D, Ascenzi P, Coletta M
Antioxidants (Basel). 2024; 13(6).
PMID: 38929104
PMC: 11201058.
DOI: 10.3390/antiox13060666.
Ascenzi P, Sbardella D, Sinibaldi F, Santucci R, Coletta M
J Biol Inorg Chem. 2016; 21(3):421-32.
PMID: 27010463
DOI: 10.1007/s00775-016-1351-1.
Schejter A, Ryan M, Blizzard E, Zhang C, Margoliash E, Feinberg B
Protein Sci. 2006; 15(2):234-41.
PMID: 16434742
PMC: 2242453.
DOI: 10.1110/ps.051825906.
Brzezinski P, Wilson M
Proc Natl Acad Sci U S A. 1997; 94(12):6176-9.
PMID: 9177190
PMC: 21022.
DOI: 10.1073/pnas.94.12.6176.
De Sanctis G, Maranesi A, Ferri T, Poscia A, Ascoli F, Santucci R
J Protein Chem. 1996; 15(7):599-606.
PMID: 8968951
DOI: 10.1007/BF01886742.
Intermediate and stable redox states of cytochrome c studied by low temperature resonance Raman spectroscopy.
Cartling B
Biophys J. 1983; 43(2):191-205.
PMID: 6311300
PMC: 1329249.
DOI: 10.1016/S0006-3495(83)84340-9.
Continuous flow-resonance Raman spectroscopy of an intermediate redox state of cytochrome C.
Forster M, Hester R, Cartling B, WILBRANDT R
Biophys J. 1982; 38(2):111-6.
PMID: 6284263
PMC: 1328885.
DOI: 10.1016/S0006-3495(82)84537-2.
Chemical modification of the haem propionate of cytochrome c.
Timkovich R
Biochem J. 1980; 185(1):47-57.
PMID: 6246879
PMC: 1161268.
DOI: 10.1042/bj1850047.
The reduction of carboxymethyl-cytochrome c by chromous ions.
Brittain T, Wilson M, Greenwood C
Biochem J. 1974; 141(2):455-61.
PMID: 4375979
PMC: 1168099.
DOI: 10.1042/bj1410455.
Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers.
Dupre S, Brunori M, Wilson M, Greenwood C
Biochem J. 1974; 141(1):299-304.
PMID: 4375972
PMC: 1168077.
DOI: 10.1042/bj1410299.
Haem ligands of the ferricytochrome c of Ustilago sphaerogena.
Vinogradov S, Bitar K, Lowenkron S
Biochem J. 1974; 139(3):547-53.
PMID: 4368759
PMC: 1166319.
DOI: 10.1042/bj1390547.
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
Wilgus H, Stellwagen E
Proc Natl Acad Sci U S A. 1974; 71(7):2892-4.
PMID: 4368392
PMC: 388578.
DOI: 10.1073/pnas.71.7.2892.
Separate intramolecular pathways for reduction and oxidation of cytochrome c in electron transport chain reactions.
MARGOLIASH E, Ferguson-Miller S, Tulloss J, Kang C, Feinberg B, Brautigan D
Proc Natl Acad Sci U S A. 1973; 70(11):3245-9.
PMID: 4361686
PMC: 427209.
DOI: 10.1073/pnas.70.11.3245.
Effect of steady illumination on the binding of carbon monoxide by carboxymethylated cytochrome c.
Wilson M, Brunori M, Bonaventura J, Bonaventura C
Biochem J. 1973; 131(4):863-5.
PMID: 4352917
PMC: 1177548.
DOI: 10.1042/bj1310863.
Chemical modification of the haem propionate of cytochrome c. A re-evaluation of the reaction of cytochrome c with a water-soluble carbodi-imide.
Mathews A, Brittain T
Biochem J. 1986; 240(1):181-7.
PMID: 3030276
PMC: 1147391.
DOI: 10.1042/bj2400181.
The binding characteristics of the cytochrome c iron.
SCHEJTER A, Plotkin B
Biochem J. 1988; 255(1):353-6.
PMID: 2848510
PMC: 1135229.
Some reactions of carbon monoxide and oxygen with carbodi-imide-modified cytochrome c.
Mathews A, Brittain T
Biochem J. 1991; 276 ( Pt 1):121-4.
PMID: 1645525
PMC: 1151152.
DOI: 10.1042/bj2760121.
Ligand binding to ferrocytochrome c at high pH.
Moore T, Greenwood C, Wilson M
Biochem J. 1975; 147(2):335-41.
PMID: 241325
PMC: 1165447.
DOI: 10.1042/bj1470335.
The preparation and some properties of mammalian cytochrome c modified with 2-hydroxy-5-nitrobenzyl bromide.
Brittain T, Greenwood C
Biochem J. 1975; 147(2):253-8.
PMID: 241320
PMC: 1165438.
DOI: 10.1042/bj1470253.
Fast reactions in carbon monoxide binding to heme proteins.
Alberding N, Austin R, Chan S, Eisenstein L, Frauenfelder H, Good D
Biophys J. 1978; 24(1):319-34.
PMID: 213136
PMC: 1473872.
DOI: 10.1016/S0006-3495(78)85380-6.
