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. Author manuscript; available in PMC: 2008 Aug 15.
Published in final edited form as: Gene. 2007 May 10;398(1-2):123–131. doi: 10.1016/j.gene.2007.02.050

Table 2. Intrinsic oxygen affinities and anaerobic redox potentials of bottlenose dolphin Hb and adult human Hb in anion-free 0.05 M HEPES buffer at pH 7.5, 20°C, and consequences of adding inorganic or organic anionic effectors.

Redox potentials are given vs NHE and were determined in the presence of a cationic mediator, 0.5 mM Ru(NH3)6. Entries are for Hb from Buster, which has a single type of Hb, and for the “Mixed” Bottlenose Dolphin Hbs of Peak II, which contained one type of α chains and three types of β chains. The dolphin Hbs in the presence of IHP oxidized rather quickly. They exhibited somewhat lower oxygen affinities in the presence of IHP (the higher P50 values listed) when measured in the presence of a cocktail of reagents developed for enzymatic heme reduction (Imai, 1982).

Protein and effectors Oxygenation Log P50 Oxidation E1/2
Buster Bottlenose Dolphin Hb 0.20 76
with 0.2 M Cl 0.53 105
with 2.5−10 fold excess IHP 1. 3−1.6 119
Mixed Bottlenose Dolphin Hbs 0.20 57
with 0.2 M Cl 0.58 96
with 2.5−10 fold excess IHP 1. 3−1.6 108
Adult Human Hb (HbA0) −0.02 72
with 0.2 M Cl 0.25 103
with 2.5−10 fold excess IHP 1.66 127