Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography.

ABSTRACT: The protonation states of the histidine residues key to the function of deoxy (T-state) human hemoglobin have been investigated using neutron protein crystallography. These residues can reversibly bind protons, thereby regulating the oxygen affinity of hemoglobin. By examining the OMIT F(o)-F(c) and 2F(o)-F(c) neutron scattering maps, the protonation states of 35 of the 38 His residues were directly determined. The remaining three residues were found to be disordered. Surprisingly, seven pairs of His residues from equivalent α or β chains, αHis20, αHis50, αHis58, αHis89, βHis63, βHis143 and βHis146, have different protonation states. The protonation of distal His residues in the α(1)β(1) heterodimer and the protonation of αHis103 in both subunits demonstrates that these residues may partic

SUBMITTER: Kovalevsky A 

PROVIDER: S-EPMC2967419 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature