Document Detail


Hydrogen Bond Strength Modulates the Mechanical Strength of Ferric-thiolate Bonds in Rubredoxin.
MedLine Citation:
PMID:  22309227     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
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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