Publication
Title
Ligation tunes protein reactivity in an ancient haemoglobin : kinetic evidence for an allosteric mechanism in **Methanosarcina acetivorans** protoglobin
Author
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.
Language
English
Source (journal)
PLoS ONE
Publication
2012
ISSN
1932-6203
Volume/pages
7:3(2012), p. e33614,1-e33614,12
Article Reference
e33614
ISI
000303894900033
Medium
E-only publicatie
Full text (Publisher's DOI)
Full text (open access)
UAntwerpen
Faculty/Department
Research group
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 03.07.2012
Last edited 10.06.2017
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