Functional implications of the proximal site hydrogen bonding network in Vitreoscilla hemoglobin (VHb): Role of Tyr95 (G5) and Tyr126 (H12)

@article{Kaur2008FunctionalIO,
  title={Functional implications of the proximal site hydrogen bonding network in Vitreoscilla hemoglobin (VHb): Role of Tyr95 (G5) and Tyr126 (H12)},
  author={R. Kaur and Sandhya Ahuja and A. Anand and Balwinder Singh and B. Stark and D. Webster and K. Dikshit},
  journal={FEBS Letters},
  year={2008},
  volume={582}
}
Although Vitreoscilla hemoglobin (VHb) carries a conventional globin fold, its proximal site geometry is unique in having a hydrogen‐bonding network between proximal site residues, HisF8‐TyrG5‐GluH23 and TyrG5‐TyrH12. TyrG5 and TyrH12 were mutated to study their relevance in VHb function. VHb G5 mutants (Tyr95Phe and Tyr95Leu showed no stable oxyform and nitric oxide dioxygenase activity, whereas, VHb H12 mutants (Tyr126Phe and Tyr126Leu) displayed little change in their oxygen affinity… Expand
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