Characterization of hemopexin and its interaction with heme by differential scanning calorimetry and circular dichroism.


Abstract

Hemopexin is a plasma glycoprotein that has two structural domains (I and II) and binds and transports heme particularly to liver cells. Differential scanning calorimetry (DSC) studies show that hemopexin is largely stabilized by heme, which binds exclusively to domain I. The melting temperature (Tm) of heme-hemopexin is 66.4 +/- 0.7 degrees C as compared with 53.9 +/- 0.3 degrees C for apohemopexin, and this Tm increase is accompanied by a 100 kcal increase in molar enthalpy. Heme stabilizes hemopexin by stabilizing domain I. This is demonstrated by the 26 degrees C increase in Tm from 51.9 +/- 0.3 to 77.6 +/- 0.6 degrees C and the over 3-fold increase in molar enthalpy when domain I associates with heme. A moderate change in domain I secondary structure is indicated by an increase in negative molar ellipticity at 206 nm. However, there is no net effect on the secondary structure of holo-hemopexin caused by heme binding as indicated by both far-UV circular dichroism (CD) and Fourier-transform infrared spectra. The characteristic positive ellipticity of hemopexin at 233 nm, ascribed to tryptophan residues in domain II, is dramatically increased, suggesting a change in teritary structure for domain II of hemopexin. DSC and CD results show that isolated domain I and domain II interact both in the presence and absence of heme. Moreover, domain II destabilizes heme-domain I, which may be an important factor in facilitating heme release to the hemopexin receptor.(ABSTRACT TRUNCATED AT 250 WORDS) Study holds ProTherm entries: 4582 Extra Details: plasma glycoprotein; structural domains; heme-hemopexin;,secondary structure;

Submission Details

ID: Yr7iWEtG4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:26 p.m.

Version: 1

Publication Details
Wu ML;Morgan WT,Biochemistry (1993) Characterization of hemopexin and its interaction with heme by differential scanning calorimetry and circular dichroism. PMID:8343510
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1HXN 1995-10-15 1.8 1.8 ANGSTROMS CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF RABBIT SERUM HEMOPEXIN
1QHU 1999-10-06 2.3 MAMMALIAN BLOOD SERUM HAEMOPEXIN DEGLYCOSYLATED AND IN COMPLEX WITH ITS LIGAND HAEM
4RT6 2016-05-18 2.8 Structure of a complex between hemopexin and hemopexin binding protein
1QJS 2000-02-03 2.9 mammalian blood serum haemopexin glycosylated-native protein and in complex with its ligand haem

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Hemopexin P20058 HEMO_RABIT