Hydrogen bond strength modulates the mechanical strength of ferric-thiolate bonds in rubredoxin.
It has long been recognized that hydrogen bonds formed by protein backbone amides with cysteinyl S(γ) 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···S(γ) 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···S(γ) hydrogen bonds as reflected by the midpoint reduction potential, providing direct evidence that N-H···S(γ) 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.
Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z1 Canada.
Peng
P
Zheng
Shin-ichi J
SJ
Takayama
A Grant
AG
Mauk
Hongbin
H
Li
D004563:Electrochemistry; D005290:Ferric Compounds / Q000737:chemistry*; D006860:Hydrogen Bonding; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D015202:Protein Engineering; D012416:Rubredoxins / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D005290:Ferric Compounds; D012416:Rubredoxins; D013438:Sulfhydryl Compounds