| Hydrogen Bond Strength Modulates the Mechanical Strength of Ferric-thiolate Bonds in Rubredoxin. | |
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MedLine Citation:
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PMID: 22309227 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Peng Zheng; Shin-Ichi J Takayama; A Grant Mauk; Hongbin Li |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-2-6 |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: - ISSN: 1520-5126 ISO Abbreviation: - Publication Date: 2012 Feb |
Date Detail:
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Created Date: 2012-2-7 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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