Sequential proton NMR assignments of iron(II) cytochrome c551 from Pseudomonas aeruginosa

Autor:	David J. Detlefsen, V. Thanabal, Vincent L. Pecoraro, Gerhard Wagner
Rok vydání:	1990
Předmět:	Hemeprotein Cytochrome biology Chemistry Stereochemistry Cytochrome c Biochemistry chemistry.chemical_compound Amide Side chain Proton NMR biology.protein Two-dimensional nuclear magnetic resonance spectroscopy Heme
Zdroj:	Biochemistry. 29:9377-9386
ISSN:	1520-4995 0006-2960
DOI:	10.1021/bi00492a011
Popis:	Sequence-specific 1H NMR resonance assignments for all but the C-terminal Lys 82 are reported for iron(II) cytochrome c551 from Pseudomonas aeruginosa at 25 degrees C and pH = 6.8. Spin systems were identified by using TOCSY and DQF-COSY spectra in 2H2O and 1H2O. Sequential assignments were made by using NOESY connectivities between adjacent amide, alpha, and beta protons. Resonances from several amino acids including His 16, Gly 24, Ile 48, and Met 61 experience strong ring-current shifts due to their placement near the heme. All heme protons, including the previously unassigned propionates, have been identified. Preliminary analysis of sequential and medium-range NOEs provides evidence for substantial amounts of helix in the solution structure. Long-range NOEs indicate that the folds in solution and crystal structures are similar. For one aromatic side chain (Tyr 27) that is close to the heme group we found a transition from hindered ring rotation at low temperature to rapid rotation at high temperature.
Databáze:	OpenAIRE
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