PMID: 5132Apr 14, 1976

Heme-linked proton dissociation of carbon monoxide complexes of myoglobin and peroxidase

Biochimica Et Biophysica Acta
Y HayashiI Yamazaki


It was found from spectrophotometric titration and proton balance measurement that the pKa value of a heme-linked protonation group of horseradish ferro-peroxidase C (donor:H2O2 oxidoreductase, EC shifted from 7.25 to 8.25 upon combination with CO. The spectrophotometric titration experiment with myoglobin also revealed the presence of a heme-linked protonation group, the pKa value being 5.57 in myoglobin and 5.67 in the CO-myoglobin complex. It was concluded that the distinct shift of the pKa value in the case of peroxidase was attributable to the presence of a hydrogen bond between the sixth ligand and the distal base. The difference in the strength of such hydrogen bonding between peroxidase and myoglobin was discussed.


Jan 20, 1975·Biochemical and Biophysical Research Communications·A Lanir, A Schejter
Jul 1, 1975·Archives of Biochemistry and Biophysics·H YamadaI Yamazaki
Mar 14, 1972·Biochemistry·S A RudolphS J Gill
Dec 1, 1974·Archives of Biochemistry and Biophysics·H Yamada, I Yamazaki
Jul 12, 1972·Journal of the American Chemical Society·R B Moon, J H Richards
Jan 22, 1966·Nature·C L NobbsJ C KENDREW
Nov 1, 1966·Biochemistry·D DuffeyG Czerlinski
Feb 1, 1967·Biochemistry·H B Dunford, R A Alberty
Oct 1, 1958·Archives of Biochemistry and Biophysics·A ROSSI-FANELLI, E ANTONINI
Jan 1, 1964·Journal of Molecular Biology·L STRYERH C WATSON
Oct 15, 1958·Proceedings of the National Academy of Sciences of the United States of America·P George, R L Lyster


Apr 17, 1979·Biochemistry·J P OhmsJ S Cohen
Sep 28, 1982·Biochemistry·W DosterK T Yue
Mar 20, 1987·Journal of Molecular Biology·W DosterE Shyamsunder
Sep 1, 1980·European Journal of Biochemistry·Y Sugawara, K Shikama
Apr 1, 1977·CRC Critical Reviews in Food Science and Nutrition·G G Giddings

Related Concepts

Carbon Monoxide
Hydrogen-Ion Concentration
Plasma Protein Binding Capacity

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