Ontology highlight
ABSTRACT:
SUBMITTER: Zhang L
PROVIDER: S-EPMC3561710 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Zhang Lei L Anderson J L Ross JL Ahmed Ismail I Norman Jessica A JA Negron Christopher C Mutter Andrew C AC Dutton P Leslie PL Koder Ronald L RL
Biochemistry 20111108 47
We report the mutational analysis of an artificial oxygen transport protein, HP7, which operates via a mechanism akin to that of human neuroglobin and cytoglobin. This protein destabilizes one of two heme-ligating histidine residues by coupling histidine side chain ligation with the burial of three charged glutamate residues on the same helix. Replacement of these glutamate residues with alanine, which is uncharged, increases the affinity of the distal histidine ligand by a factor of 13. Paradox ...[more]