Introduction of a new regulatory mechanism into human hemoglobin

• Published in: Biophysical chemistry Vol. 98; no. 1; pp. 115 - 126
• Main Authors: Fronticelli, Clara, Bobofchak, Kevin M., Karavitis, Michael, Sanna, Maria Teresa, Brinigar, William S.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 10.07.2002
• Subjects: Animals; Apoproteins - chemistry; Apoproteins - metabolism; Autoxidation; Binding Sites; Bovine hemoglobin; Cattle; Chlorides - chemistry; Chlorides - metabolism; Circular Dichroism; Heme transfer; Hemoglobins - chemistry; Hemoglobins - genetics; Hemoglobins - metabolism; Humans; Hydrogen-Ion Concentration; Kinetics; Low intrinsic oxygen affinity; Mutagenesis; Myoglobin - chemistry; Myoglobin - metabolism; Oxygen - metabolism; Protein Conformation; Protein Denaturation; Recombinant hemoglobin; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Temperature; PB4: hemoglobin with mutations β(V1M+H2+T4I+P5A); Heme transfer; 2,3-DPG: 2,3 Diphosphoglycerate; Recombinant hemoglobin; Hb: hemoglobin; Circular dichroism; PB5: hemoglobin with mutations β(V1M+H2+T4I+P5A+A76K); PB5 control: hemoglobin with mutations β (V1M+H2+P5A+A76K); Autoxidation; IHP: inositol hexaphosphate; rβHbA: human hemoglobin with recombinant β-chains; PB6: hemoglobin with mutations β(V1M+H2+T4I+P5A+K8Q+A76K); Bovine hemoglobin; Low intrinsic oxygen affinity; apoMb: apomyoglobin; PB2: hemoglobin with mutations β(V1M+H2); HbA: human hemoglobin; HbBv: bovine hemoglobin

Previous studies on bovine hemoglobin (HbBv) have suggested amino acid substitutions, which might introduce into human hemoglobin (HbA) functional characteristics of HbBv, namely a low intrinsic oxygen affinity regulated by Cl −. Accordingly, we have constructed and characterized a multiple mutant,...