Correction: Allostery in the nitric oxide dioxygenase mechanism of flavohemoglobin
Year: 2021
Type: erratum
Abstract: Allostery in the nitric oxide dioxygenase mechanism of flavohemoglobinJournal of Biological ChemistryVol. 296PreviewThe substrates O2 and NO cooperatively activate the NO dioxygenase function of Escherichia coli flavohemoglobin. Steady-state and transient kinetic measurements support a structure-based mechanistic model in which O2 and NO movements and conserved amino acids at the E11, G8, E2, E7, B10, and F7 positions within the globin domain control activation. In the cooperative and allosteric mechanism, O2 migrates to the catalytic heme site via a long hydrophobic tunnel and displaces LeuE11 away from the ferric iron, which forces open a short tunnel to the catalytic site gated by the ValG8/IleE15 pair and LeuE11. Full-Text PDF Open Access VOLUME 296 (2021) ARTICLE NUMBER 100186 In the present article on page 7 it states “rate constant approaching the value of 6.9 × 1010 M−1 s−1 for the bimolecular reaction of NO and free O2− (48).” Instead it should read “rate constant exceeding the value of (6.7 ± 0.9) × 109 M−1 s−1 for the bimolecular reaction of NO and free O2− (48).”
Source: Journal of Biological Chemistry
Authors: Anne M. Gardner, Paul R. Gardner
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,500
OpenAlex ID: W3150657614