Side chain mobility as monitored by CH-CH cross correlation: the example of cytochrome b5.
The mobility of betaCH2 moieties in oxidized and reduced cytochrome b5 was studied by analyzing the 13C relaxation of the J-split components, in terms of C-H dipole-C-H dipole cross correlation rates. A 2D 13C-1H experiment is proposed to measure these rates that provide the internal effective reorientation correlation time for each CH2 moiety. It is found that higher mobility is present in the alpha helices forming the heme pocket. On the contrary, the beta strands, which form the hydrophobic core of the molecule, have the lowest mobility. The general pattern is the same for the oxidized and reduced species, indicating that any oxidation-dependent property detected for backbone NH moieties does not affect the CH2 mobility.
Banci
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L
Magnetic Resonance Center (CERM), University of Florence, Sesto Fiorentino, Italy.
Bertini
I
I
Felli
I C
IC
Hajieva
P
P
Viezzoli
M S
MS
D001426:Bacterial Proteins / Q000737:chemistry*; D015786:Cytochromes b5 / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D006418:Heme / Q000737:chemistry; D008958:Models, Molecular; D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011487:Protein Conformation
D001426:Bacterial Proteins; D006418:Heme; D015786:Cytochromes b5