@article { ISI:000301550800050,
	title = {Hydrogen Bond Strength Modulates the Mechanical Strength of Ferric-Thiolate Bonds in Rubredoxin},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {134},
	number = {9},
	year = {2012},
	month = {MAR 7},
	pages = {4124-4131},
	abstract = {It has long been recognized that hydrogen bonds formed by protein backbone amides with cysteinyl S-gamma 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 center dot center dot center dot S-gamma 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 center dot center dot center dot S-gamma hydrogen bonds as reflected by the midpoint reduction potential, providing direct evidence that N-H center dot center dot center dot S-gamma 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.},
	issn = {0002-7863},
	doi = {10.1021/ja2078812},
	author = {Zheng, Peng and Takayama, Shin-ichi J. and Mauk, A. Grant and Li, Hongbin}
}
