2012 journal article
Thin-layer spectroelectrochemistry of the Fe(III)/Fe(II) redox reaction of dehaloperoxidase-hemoglobin
JOURNAL OF ELECTROANALYTICAL CHEMISTRY, 668, 37–43.
author keywords: Dehaloperoxidase; Hemoglobin; Fe(III)/Fe(II) reduction potential; Gibbs free energy analysis; Distal histidine conformation; Redox thermodynamic square scheme
TL;DR:
A thermodynamic cycle that links the conformational change to electron transfer is shown to be consistent with a positive shift in reduction potential if the open conformation is differentially favored by the Fe(II) state, a proposal that is supported by the available crystallographic data.
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Added: August 6, 2018
Dehaloperoxidase-hemoglobin (DHP A; isoenzyme A) is a globin from the annelid Amphitrite ornata that displays enhanced peroxidase activity compared to other myoglobins and hemoglobins. In this study, anaerobic thin-layer spectroelectrochemistry was used to measure formal reduction potentials (E°′) for the Fe(III)/Fe(II) redox couple of DHP A from pH 5.0 to pH 7.0. The value of E°′ determined at pH 7.0 (100 mM potassium phosphate buffer under ambient temperature), +0.202 ± 0.006 V vs SHE, gives DHP A the most positive Fe(III)/Fe(II) reduction potential among known intracellular globins (approximately 150 mV and 50 mV higher than typical myoglobins and hemoglobins, respectively). This finding is particularly distinctive in light of DHP A's enhanced peroxidase activity, a function that is commonly carried out from the Fe(III) state, which is favored by more negative reduction potentials. For example, horseradish peroxidase has a formal potential that falls 0.47 V negative of the DHP A value. Using available crystal structures, two major energetic factors involving the distal histidine (H55) have been identified that appear to account for the unusually positive DHP A reduction potential. First, H55, which is positioned ∼1 Å further away from the heme iron than distal histidines in hemoglobin and myoglobin, displays a diminished capacity to serve as the hydrogen bond acceptor for a ligated water molecule, resulting in destabilization of the Fe(III) state relative to a common globin. The more distant positioning of H55 from the heme iron also imparts to it a conformational flexibility, which is linked to the electron transfer reaction. In its internal (closed) conformation, H55 hydrogen bonds with and stabilizes an iron-ligated H2O molecule, whereas in its external (open) conformation, H55 hydrogen bonds to a heme propionate resulting in a 5-coordinate heme iron. A thermodynamic cycle that links the conformational change to electron transfer is shown to be consistent with a positive shift in reduction potential if the open conformation is differentially favored by the Fe(II) state, a proposal that is supported by the available crystallographic data.