Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 241 to 241 of 241

Publication Record

Connections

Nitric oxide induced conformational changes in opossum hemoglobin.
John ME, Waterman MR
(1979) J Biol Chem 254: 11953-7
MeSH Terms: Amino Acids, Animals, Electron Spin Resonance Spectroscopy, Hemoglobin A, Hemoglobins, Humans, Hydrogen-Ion Concentration, Kinetics, Nitric Oxide, Opossums, Oxyhemoglobins, Protein Binding, Protein Conformation, Species Specificity
Show Abstract · Added February 12, 2015
Opossum hemoglobin assumes a T quaternary structure upon NO ligation in the absence of organic phophates at pH 6.7. In addition, stripped opossum hemoglobin exhibits a low oxygen affinity when compared to human hemoglobin and a pH-dependent heme-heme interaction with an n value of 2.14 at pH 7.0 and 2.46 at pH 7.35. These observations indicate that opossum hemoglobin may have a destabilized oxy structure when compared to hemoglobin A due to differences in primary structure. Thus, the strong trans ligand effect of nitric oxide is able to disrupt the proximal histidine-iron bond in the alpha-hemes triggering a conformational transition to the T state. Absence of a distal histidine in the alpha-subunits and, therefore an impaired donor acceptor interaction with the sixth ligand, could contribute to the lack of stability of the R quaternary structure in opossum nitrosylhemoglobin. The reduced oxygen affinity of opossum hemoglobin may be compensated for by other physiological factors such as a reduced phosphate effect.
0 Communities
1 Members
0 Resources
14 MeSH Terms