Two-dimensional 1H NMR spectra of ferricytochrome c551 from Pseudomonas aeruginosa.
The full assignment of 1H NMR signals of heme proton resonances of ferricytochrome c551 from Pseudomonas aeruginosa has been performed by means of 2D NMR experiments. This technique allows the complete and unequivocal assignment of all heme resonances, including methylene resonances of the propionic groups, directly implicated in the pH dependence of the redox properties of cytochrome c551.
Moratal
J M
JM
Department of Inorganic Chemistry, University of Valencia, Italy.
Donaire
A
A
Salgado
J
J
Jiménez
H R
HR
Castells
J
J
Piccioli
M
M
D001426:Bacterial Proteins / Q000737:chemistry; D003574:Cytochrome c Group / Q000737:chemistry*; D005290:Ferric Compounds; D006418:Heme / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D011550:Pseudomonas aeruginosa / Q000737:chemistry*
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D005290:Ferric Compounds; D006418:Heme; C017167:cytochrome C(551)