Solution structure of mitochondrial cytochrome c. II. 1H nuclear magnetic resonance of ferrocytochrome c.
The 1H nuclear magnetic resonance spectrum of tuna ferrocytochrome c has been studied and the resonances of all 49 amino acid methyl groups have been assigned to specific absorption lines. In comparison with resonance assignments in the ferricytochrome c spectrum, the secondary shifts of resonances of ferrocytochrome c are smaller and the identification of characteristic spin-systems from comparison of spectra from homologous proteins more difficult. For this reason, two-dimensional nuclear magnetic resonance exchange correlated spectroscopy has been used to correlate the assigned resonances of tuna ferricytochrome c with previously unassigned resonances of tuna ferrocytochrome c.
Moore
G R
GR
Robinson
M N
MN
Williams
G
G
Williams
R J
RJ
D000595:Amino Acid Sequence; D000818:Animals; D002175:Candida; D010856:Columbidae; D003574:Cytochrome c Group; D006736:Horses; D007798:Lampreys; D007614:Macropodidae; D009682:Magnetic Resonance Spectroscopy; D008928:Mitochondria / Q000032:analysis*; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae; D012996:Solutions; D014413:Tuna
D003574:Cytochrome c Group; D012996:Solutions