Proton resonance assignments for Pseudomonas aeruginosa ferrocytochrome c-551.
A comparison between two sets of resonance assignments for ferrocytochrome c-551 from Pseudomonas aeruginosa reveals that major differences can be explained by pH effects. In turn, these reveal side chain protonation events in c-551 that markedly influence spectra. The behavior of resonances in a homologous protein from Pseudomonas stutzeri help to clarify ambiguities in the P. aeruginosa case. A corrected and completed set of proline assignments is presented. Labile side chain protons in residue 47, which hydrogen bonds to the inner heme propionate, appear to be in fast exchange with the solvent.
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Department of Chemistry, University of Alabama, Tuscaloosa 35487.
Timkovich
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003574:Cytochrome c Group / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011392:Proline; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000378:metabolism*
D001426:Bacterial Proteins; D003574:Cytochrome c Group; C017167:cytochrome C(551); D011392:Proline