Document Detail

Hydrogen Bond Strength Modulates the Mechanical Strength of Ferric-thiolate Bonds in Rubredoxin.
MedLine Citation:
PMID:  22309227     Owner:  NLM     Status:  Publisher    
It has long been recognized that hydrogen bonds formed by protein backbone amides with cysteinyl Sγ atoms play important roles in modulating the functional and structural properties of the iron-sulfur centers in proteins. Here we use single molecule atomic force microscopy, cyclic voltammetry and protein engineering techniques to investigate directly how the strength of N…H-Sγ hydrogen bonds in the secondary coordination sphere affects the mechanical stability of Fe(III)-thiolate bonds of rubredoxin. Our results show that the mechanical stability of Fe(III)-thiolate bonds in rubredoxin correlates with the strength of N…H-Sγ hydrogen bonds as reflected by the midpoint reduction potential, providing direct evidence that N…H-Sγ hydrogen bonds play important roles in modulating the mechanical and kinetic properties of the Fe(III)-thiolate bonds of iron-sulfur proteins and corroborating the important roles of the protein environment in tuning the properties of metal-thiolate bonds.
Peng Zheng; Shin-Ichi J Takayama; A Grant Mauk; Hongbin Li
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-2-6
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  -     ISSN:  1520-5126     ISO Abbreviation:  -     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-2-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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