TY - JOUR
T1 - Backbone dynamics and hydrogen exchange of Pseudomonas aeruginosa ferricytochrome C551
AU - Russell, Brandy S.
AU - Zhong, Linghao
AU - Bigotti, Maria Giulia
AU - Cutruzzolà, Francesca
AU - Bren, Kara L.
N1 - Funding Information:
Acknowledgements The authors thank Linda Thöny-Meyer for the gift of pEC86, and Arthur G. Palmer III, for providing Curvefit and Modelfree 4.01. Maurizio Brunori is thanked for facilitating this collaboration and providing insightful comments on this manuscript. This work was funded by a National Institutes of Health grant to K.L.B. (GM63170).
PY - 2003/1
Y1 - 2003/1
N2 - A model-free analysis of Pseudomonas aeruginosa ferricytochrome C551 dynamics based on 15N R1 15N R2 and {1H}-15N heteronuclear nuclear Overhauser effect data is reported. The protein backbone is highly rigid (2> = 0.924±0.005) and displays little variation in picosecond-nanosecond time scale dynamics over the structure. The loop structure containing the axial methionine ligand (loop 3) displays anomalous rigidity, which is attributed to its high proline content. Also reported are protection factors calculated from hydrogen-exchange rates. These data reveal that loop 3 residues, including the axial methionine, are protected from exchange as a result of long-range hydrogen-bonding interactions. These results are contrasted with data reported for Saccharomyces cerevisiae iso-1-ferricytochrome c, which displays higher overall flexibility ( = 0.80±0.07), greater variation of dynamics as a function of structure, and low protection factors for loop 3. This analysis reveals that heme proteins with similar functions and topologies may display diverse dynamical properties. Electronic supplementary material is available if you access this article at http://dx.doi.org/10.1007/s00775-002-0401-z. On that page (frame on the left side), a link takes you directly to the supplementary material.
AB - A model-free analysis of Pseudomonas aeruginosa ferricytochrome C551 dynamics based on 15N R1 15N R2 and {1H}-15N heteronuclear nuclear Overhauser effect data is reported. The protein backbone is highly rigid (2> = 0.924±0.005) and displays little variation in picosecond-nanosecond time scale dynamics over the structure. The loop structure containing the axial methionine ligand (loop 3) displays anomalous rigidity, which is attributed to its high proline content. Also reported are protection factors calculated from hydrogen-exchange rates. These data reveal that loop 3 residues, including the axial methionine, are protected from exchange as a result of long-range hydrogen-bonding interactions. These results are contrasted with data reported for Saccharomyces cerevisiae iso-1-ferricytochrome c, which displays higher overall flexibility ( = 0.80±0.07), greater variation of dynamics as a function of structure, and low protection factors for loop 3. This analysis reveals that heme proteins with similar functions and topologies may display diverse dynamical properties. Electronic supplementary material is available if you access this article at http://dx.doi.org/10.1007/s00775-002-0401-z. On that page (frame on the left side), a link takes you directly to the supplementary material.
UR - http://www.scopus.com/inward/record.url?scp=0037259914&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037259914&partnerID=8YFLogxK
U2 - 10.1007/s00775-002-0401-z
DO - 10.1007/s00775-002-0401-z
M3 - Article
C2 - 12459911
AN - SCOPUS:0037259914
SN - 0949-8257
VL - 8
SP - 156
EP - 166
JO - Journal of Biological Inorganic Chemistry
JF - Journal of Biological Inorganic Chemistry
IS - 1-2
ER -