Document Detail


The reactions of neuroglobin with CO: evidence for two forms of the ferrous protein.
MedLine Citation:
PMID:  16684569     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The normally hexa coordinate ferrous form of neuroglobin binds CO by replacement of the heme-linked distal histidine residue. We have studied this reaction in detail using stopped flow techniques. The reaction time courses are complex at all the wavelengths studied. Specifically the reaction with CO occurs in two temporally separable phases, each of which shows a hyperbolic dependence of rate on CO concentration, indicating they each arise from histidine replacement by CO. Analysis of the observed rates as a function of the CO concentration, measured in the pH range 6.0-8.0, allows us to determine both the rate of histidine-heme ligand binding and dissociation for each of the two forms of the protein present in solution at each pH value. The pH dependence of the histidine association and dissociation rates is complex, as are the derived equilibrium constants for distal histidine binding. The spectral change associated with each reaction phase is very similar and independent of the CO concentration, showing that the two protein forms responsible for the two observed kinetic processes are not in equilibrium on the time scale of our investigations. Our data suggests that, unlike many other heme proteins, neuroglobin displays complex reactivity with ligands in the ferrous form due to heme rotational disorder, as has previously been reported for the ferric form of the protein.
Authors:
Angela Fago; Antony J Mathews; Sylvia Dewilde; Luc Moens; Thomas Brittain
Related Documents :
18439429 - Thermostability, solvent tolerance, catalytic activity and conformation of cofactor mod...
10218639 - Cyclooxygenase dependent release of heme from microsomal hemeproteins correlates with i...
19300529 - Effects of active site mutations in haemoglobin i from lucina pectinata: a molecular dy...
10413489 - Proton nmr investigation of the heme active site structure of an engineered cytochrome ...
12598659 - Non-heme iron enzymes: contrasts to heme catalysis.
6639949 - Circular dichroism studies of low-spin ferric cytochrome p-450cam ligand complexes.
20097169 - Evidence for dimeric bace-mediated app processing.
3183069 - Relationship of subgingival microbial complexes to clinical features at the sampled sites.
24417449 - Rapid identification of keap1-nrf2 small molecule inhibitors through structure-based vi...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-04-05
Journal Detail:
Title:  Journal of inorganic biochemistry     Volume:  100     ISSN:  0162-0134     ISO Abbreviation:  J. Inorg. Biochem.     Publication Date:  2006 Aug 
Date Detail:
Created Date:  2006-07-10     Completed Date:  2006-10-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7905788     Medline TA:  J Inorg Biochem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1339-43     Citation Subset:  IM    
Affiliation:
Zoophysiology, Institute of Biological Sciences, C.F. Møllers Alle 131, Aarhus University, DK-8000 Aarhus C, Denmark.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Carbon Monoxide / chemistry*,  metabolism
Globins / chemistry*,  metabolism
Histidine / chemistry,  metabolism
Hydrogen-Ion Concentration
Iron / chemistry*
Kinetics
Ligands
Mice
Nerve Tissue Proteins / chemistry*,  metabolism
Oxidation-Reduction
Protein Conformation
Chemical
Reg. No./Substance:
0/Ligands; 0/Nerve Tissue Proteins; 0/neuroglobin; 630-08-0/Carbon Monoxide; 71-00-1/Histidine; 7439-89-6/Iron; 9004-22-2/Globins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Characterization and crystal structure of cadmium(II) halide complexes with amino acids and their de...
Next Document:  3D-QSAR study for DNA cleavage proteins with a potential anti-tumor ATCUN-like motif.