Hydrogen bond strength modulates the mechanical strength of ferric-thiolate bonds in rubredoxin

Journal of the American Chemical Society

Volumn 134, Issue 9, 2012, Pages 4124-4131

  Zheng, Peng ^a   Takayama, Shin Ichi J ^a   Mauk, A Grant ^a   Li, Hongbin ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

COORDINATION SPHERE; IRON-SULFUR PROTEINS; KINETIC PROPERTIES; METAL-THIOLATE; PROTEIN BACKBONE; PROTEIN ENGINEERING; REDUCTION POTENTIAL; RUBREDOXIN; SINGLE MOLECULE; THIOLATES;

AMIDES; ATOMIC FORCE MICROSCOPY; BOND STRENGTH (CHEMICAL); CYCLIC VOLTAMMETRY; GENETIC ENGINEERING; IRON COMPOUNDS; MECHANICAL STABILITY; PROTEINS; SULFUR;

HYDROGEN BONDS;

ALANINE; CYSTEINE; FERRIC ION; GLYCINE; IRON; PROLINE; RUBREDOXIN; SULFUR; TYROSINE;

ARTICLE; ATOMIC FORCE MICROSCOPY; CYCLIC POTENTIOMETRY; GENETIC VARIABILITY; HYDROGEN BOND; OXIDATION REDUCTION POTENTIAL; PROTEIN ENGINEERING; PROTEIN STRUCTURE; STRENGTH;

ELECTROCHEMISTRY; FERRIC COMPOUNDS; HYDROGEN BONDING; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; PROTEIN ENGINEERING; RUBREDOXINS; SULFHYDRYL COMPOUNDS;

EID: 84863276366     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja2078812     Document Type: Article

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43. c of 13 nm, at least two ferric-thiolate bonds from the same CXXC chelating motif need to be ruptured. Thus, the measured rupture force could also include contributions from unfolding of the CXXC chelating loop. However, unfolding of the CXXC loop will result in a length increment of ∼1nm, which cannot be resolved by our AFM due to the compliant polypeptide chain.
44. It is important to note that in addition to the effect of eliminating a backbone hydrogen bond or affecting the strength of the backbone hydrogen bond by the proline or glycine substitutions, it is possible that introduction of a proline or glycine also affects the flexibility of the CXXC chelating loop (proline substitution makes the loop stiffer while glycine substitution makes the loops more flexible) and thus the force needed to unfold the CXXC chelating loop. It is possible that these collective effects contribute to the observed change of the mechanical stability of ferric-thiolate bonds. Nonetheless, these possibilities point to the fact that protein environment plays important roles in modulating the mechanical stability of ferric-thiolate bonds in rubredoxin.
45. γ hydrogen bonds on the mechanical stability of ferrous-thiolate bond in rubredoxin. Previously, we used the reducing agent dithiothreitol (DTT) to measure the mechanical stability of ferrous-thiolate bond in rubredoxin. However, DTT or other reducing agents are competing ligands for ferrous/ferric ion. Thus, the measured mechanical stability of ferrous-thiolate bonds is potentially complicated by the effect of such competing ligands. Therefore, such experiments call for anaerobic environment in which AFM will be housed or an electrochemical AFM setup. Future endeavors will be required for carrying out such experiments.
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