Title
Ligation tunes protein reactivity in an ancient haemoglobin : kinetic evidence for an allosteric mechanism in **Methanosarcina acetivorans** protoglobinLigation tunes protein reactivity in an ancient haemoglobin : kinetic evidence for an allosteric mechanism in **Methanosarcina acetivorans** protoglobin
Author
Faculty/Department
Faculty of Sciences. Physics
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Research group
Biophysics and Biomedical Physics
Proteinchemistry, proteomics and epigenetic signalling(PPES)
Publication type
article
Publication
Subject
Biology
Human medicine
Source (journal)
PLoS ONE
Volume/pages
7(2012):3, p. e33614,1-e33614,12
ISSN
1932-6203
Article Reference
e33614
Carrier
E-only publicatie
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Protoglobin from Methanosarcina acetivorans (MaPgb) is a dimeric globin with peculiar structural properties such as a completely buried haem and two orthogonal tunnels connecting the distal cavity to the solvent. CO binding to and dissociation from MaPgb occur through a biphasic kinetics. We show that the heterogenous kinetics arises from binding to (and dissociation from) two tertiary conformations in ligation-dependent equilibrium. Ligation favours the species with high binding rate (and low dissociation rate). The equilibrium is shifted towards the species with low binding (and high dissociation) rates for the unliganded molecules. A quantitative model is proposed to describe the observed carbonylation kinetics.
Full text (open access)
https://repository.uantwerpen.be/docman/irua/298013/2044.pdf
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