Linearity of the hemoglobin oxidation bohr effect.

Abstract:

:The hemoglobin oxidation Bohr effect below pH 7 is essentially proportional to the fraction of hemes oxidized, just as the ligation Bohr effect is proportional to fractional heme ligation. The reported nonlinear proton release during oxidation [(1965) J. Biol. Chem. 240, 3317-3324] is shown to be an artifact resulting from the use of ferricyanide as oxidant. Published forms of the two-state allosteric transition model for hemoglobin function have used several proton linkage schemes, and none are compatible with a linear proton release upon oxidation.

authors

Hoffman BM,Bull C

doi

10.1073/pnas.73.3.800

keywords:

subject

Has Abstract

pub_date

1976-03-01 00:00:00

pages

800-3

issue

3

eissn

0027-8424

issn

1091-6490

journal_volume

73

pub_type

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