PMID: 274697Mar 1, 1978

Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand binding

Proceedings of the National Academy of Sciences of the United States of America
P W TuckerW S Caughey

Abstract

In hemoglobin Zürich the side chain of the distal arginine attaches itself to the propionate of the heme, leaving the heme pocket wide open, allowing sulfanilamides easy access to the iron, and doubling the partition coefficient between CO and O2. The replacement of the distal valine by alanine in hemoglobin Sydney leaves a large gap inside the heme pocket, which is partly filled by a water molecule bonded to the distal histidine. Hemoglobin Sydney has the same partition coefficient between CO and O2 as hemoglobin A. Replacement of the distal histidine increases the stretching frequency of CO linked to the beta heme by 6 cm-1, but replacement of the distal valine increases it by only 3 cm-1, but replacement of the distal histidine leaves the O-O stretching frequency unchanged.

References

Aug 15, 1977·Journal of Molecular Biology·R C LadnerM F Perutz
Apr 1, 1977·Journal of Physics E: Scientific Instruments·J F MallettT H Gossling
May 2, 1977·European Journal of Biochemistry·G M GiacomettiK H Winterhalter
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Oct 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·J P CollmanK S Suslick
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May 20, 1969·Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character·M F Perutz
Jan 1, 1972·Cold Spring Harbor Symposia on Quantitative Biology·M F Perutz, L F TenEyck
Mar 1, 1970·Proceedings of the National Academy of Sciences of the United States of America·H Jacob, K H Winterhalter
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Citations

Jan 1, 1981·Journal of Molecular Evolution·A E Romero-HerreraH Mizukami
Aug 15, 1979·Journal of Molecular Biology·D A Case, M Karplus
Jan 1, 1982·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·M E JohnM R Waterman
Jan 1, 1987·Journal of Pharmaceutical and Biomedical Analysis·M Cornarakis-Lentzos, P R Cowin
Nov 25, 1983·Journal of Molecular Biology·B Shaanan
Dec 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·J P CollmanK M Doxsee
Dec 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·M W MakinenW S Caughey
Oct 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·D H BuschG G Christoph
May 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·W S CaugheyM P Tucker
Oct 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·D D DlottE E DiIorio
Mar 1, 1984·Journal of Biomolecular Structure & Dynamics·A LevyJ M Rifkind
Dec 17, 1984·European Journal of Biochemistry·E E Di IorioJ Peisach
Aug 28, 1990·European Journal of Biochemistry·Y YamamotoT Suzuki
Aug 5, 1987·Biochimica Et Biophysica Acta·T Suzuki
Mar 15, 1981·Journal of Molecular Biology·J D Smit, K H Winterhalter
Oct 5, 1980·Journal of Molecular Biology·S E Phillips
Jul 25, 1981·Journal of Molecular Biology·S E PhillipsM F Perutz
Jun 3, 1986·Biochemistry·A AnsariE Shyamsunder
Jan 1, 1990·Hemoglobin·Y Ohba
Sep 28, 2010·American Journal of Hematology·Osheiza AbdulmalikJ Eric Russell
Jan 3, 1997·The Journal of Biological Chemistry·J N Rodriguez-LopezR N Thorneley
Dec 25, 2016·The Journal of Biological Chemistry·Emmanuel BisséJohn S Olson

Related Concepts

Abufne
Arginine hydrochloride
Abnormal Hemoglobins
Histidine
Ligands
Dioxygen
Protein Conformation
Structure-Activity Relationship
Valine
X-Ray Diffraction

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