Distal Regulation of Heme Binding of Heme Oxygenase-1 Mediated by Conformational Fluctuations

Biochemistry ◽  
2014 ◽  
Vol 54 (2) ◽  
pp. 340-348 ◽  
Author(s):  
Erisa Harada ◽  
Masakazu Sugishima ◽  
Jiro Harada ◽  
Keiichi Fukuyama ◽  
Kenji Sugase
Keyword(s):  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Heme Binding

Expression of the mRNA of Heme-Binding Protein 23 Is Coordinated with That of Heme Oxygenase-1 by Heme and Heavy Metals in Primary Rat Hepatocytes and Hepatoma Cells

Biochemistry ◽  
1995 ◽  
Vol 34 (41) ◽  
pp. 13407-13411 ◽  
Author(s):  
Stephan Immenschuh ◽  
Shin-ichiro Iwahara ◽  
Hiroyuki Satoh ◽  
Christina Nell ◽  
Norbert Katz ◽  
...  
Keyword(s):  
Heavy Metals ◽  
Heme Oxygenase ◽  
Binding Protein ◽  
Rat Hepatocytes ◽  
Hepatoma Cells ◽  
Heme Oxygenase 1 ◽  
Heme Binding ◽  
Primary Rat Hepatocytes ◽  
Heme Binding Protein

Crystal Structure of Rat Apo-Heme Oxygenase-1 (HO-1):  Mechanism of Heme Binding in HO-1 Inferred from Structural Comparison of the Apo and Heme Complex Forms†,‡

Biochemistry ◽  
2002 ◽  
Vol 41 (23) ◽  
pp. 7293-7300 ◽  
Author(s):  
Masakazu Sugishima ◽  
Hiroshi Sakamoto ◽  
Yoshimitsu Kakuta ◽  
Yoshiaki Omata ◽  
Shunsuke Hayashi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Heme Binding ◽  
Structural Comparison ◽  
Complex Forms

scholarly journals Dynamic and structural differences between heme oxygenase-1 and -2 are due to differences in their C-terminal regions

2019 ◽  
Vol 294 (20) ◽  
pp. 8259-8272 ◽  
Author(s):  
Brent A. Kochert ◽  
Angela S. Fleischhacker ◽  
Thomas E. Wales ◽  
Donald F. Becker ◽  
John R. Engen ◽  
...  
Keyword(s):  
Heme Oxygenase ◽  
Structural Changes ◽  
Size Exclusion ◽  
Heme Oxygenase 1 ◽  
Heme Binding ◽  
Hydrophobic Membrane ◽  
Membrane Anchor ◽  
Catalytic Core ◽  
Structural Differences ◽  
Exclusion Chromatography

Heme oxygenase (HO) catalyzes heme degradation, a process crucial for regulating cellular levels of this vital, but cytotoxic, cofactor. Two HO isoforms, HO1 and HO2, exhibit similar catalytic mechanisms and efficiencies. They also share catalytic core structures, including the heme-binding site. Outside their catalytic cores are two regions unique to HO2: a 20-amino acid–long N-terminal extension and a C-terminal domain containing two heme regulatory motifs (HRMs) that bind heme independently of the core. Both HO isoforms contain a C-terminal hydrophobic membrane anchor; however, their sequences diverge. Here, using hydrogen–deuterium exchange MS, size-exclusion chromatography, and sedimentation velocity, we investigated how these divergent regions impact the dynamics and structure of the apo and heme-bound forms of HO1 and HO2. Our results reveal that heme binding to the catalytic cores of HO1 and HO2 causes similar dynamic and structural changes in regions (proximal, distal, and A6 helices) within and linked to the heme pocket. We observed that full-length HO2 is more dynamic than truncated forms lacking the membrane-anchoring region, despite sharing the same steady-state activity and heme-binding properties. In contrast, the membrane anchor of HO1 did not influence its dynamics. Furthermore, although residues within the HRM domain facilitated HO2 dimerization, neither the HRM region nor the N-terminal extension appeared to affect HO2 dynamics. In summary, our results highlight significant dynamic and structural differences between HO2 and HO1 and indicate that their dissimilar C-terminal regions play a major role in controlling the structural dynamics of these two proteins.

scholarly journals Differential Cellular and Subcellular Localization of Heme-Binding Protein 23/Peroxiredoxin I and Heme Oxygenase-1 in Rat Liver

2003 ◽  
Vol 51 (12) ◽  
pp. 1621-1631 ◽  
Author(s):  
Stephan Immenschuh ◽  
Eveline Baumgart-Vogt ◽  
Melly Tan ◽  
Shin-Ichiro Iwahara ◽  
Giuliano Ramadori ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Heme Oxygenase ◽  
Rat Liver ◽  
Binding Protein ◽  
Heme Oxygenase 1 ◽  
Heme Binding ◽  
Heme Binding Protein ◽  
Peroxiredoxin I

Induction of HEME Oxygenase 1 reduces inflammation and fibrosis in a mouse model of chronic hepatitis

2011 ◽  
Vol 49 (01) ◽  
Author(s):  
R Barikbin ◽  
D Schwinge ◽  
C Schramm ◽  
G Tiegs ◽  
G Sass
Keyword(s):  
Chronic Hepatitis ◽  
Mouse Model ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1
Sign in / Sign up

Export Citation Format

Share Document