X-ray Crystal Structure of Human Heme Oxygenase-1 with (2R,4S)-2-[2-(4-Chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane: A Novel, Inducible Binding Mode

2009 ◽  
Vol 52 (15) ◽  
pp. 4946-4950 ◽  
Author(s):  
Mona N. Rahman ◽  
Jason Z. Vlahakis ◽  
Dragic Vukomanovic ◽  
Walter A. Szarek ◽  
Kanji Nakatsu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Binding Mode ◽  
Heme Oxygenase 1 ◽  
X Ray

scholarly journals Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin

2020 ◽  
pp. jbc.RA120.016271
Author(s):  
Rei Tohda ◽  
Hideaki Tanaka ◽  
Risa Mutoh ◽  
Xuhong Zhang ◽  
Young-Ho Lee ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Higher Plants ◽  
Fine Tuning ◽  
Titration Calorimetry ◽  
Heme Oxygenase 1 ◽  
Enzymatic Reactions ◽  
Plant Type ◽  
Higher Plant ◽  
X Ray

Heme oxygenase (HO) converts heme to carbon monoxide, biliverdin, and free iron, products that are essential in cellular redox signaling and iron recycling. In higher plants, HO is also involved in the biosynthesis of photoreceptor pigment precursors. Despite many common enzymatic reactions, the amino acid sequence identity between plant-type and other HOs is exceptionally low (~19.4 %) and amino acids that are catalytically important in mammalian HO are not conserved in plant-type HOs. Structural characterization of plant-type HO is limited to spectroscopic characterization by Electron Spin Resonance, and it remains unclear how the structure of plant-type HO differs from that of other HOs. Here, we have solved the crystal structure of Glycine max (soybean) HO-1 (GmHO-1) at 1.06 Å resolution, and carried out the Isothermal Titration Calorimetry (ITC) measurements and Nuclear Magnetic Resonance (NMR) spectroscopic studies of its interaction with ferredoxin (Fd), the plant-specific electron donor. The high-resolution X-ray structure of GmHO-1 reveals several novel structural components: an additional irregularly structured region, a new water tunnel from the active site to the surface, and a hydrogen-bonding network unique to plant-type HOs. Structurally important features in other HOs, such as His ligation to the bound heme, are conserved in GmHO-1. Based on combined data from X-ray crystallography, ITC, and NMR measurements, we propose the evolutionary fine-tuning of plant-type HOs for Fd dependency in order to allow adaptation to dynamic pH changes on the stroma side of the thylakoid membrane in chloroplast without losing enzymatic activity under conditions of fluctuating light.

scholarly journals Crystal structure of rat heme oxygenase-1 in complex with heme

FEBS Letters ◽  
2000 ◽  
Vol 471 (1) ◽  
pp. 61-66 ◽  
Author(s):  
Masakazu Sugishima ◽  
Yoshiaki Omata ◽  
Yoshimitsu Kakuta ◽  
Hiroshi Sakamoto ◽  
Masato Noguchi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1

Crystal Structure of Human Heme Oxygenase-1 in a Complex with Biliverdin†

Biochemistry ◽  
2004 ◽  
Vol 43 (13) ◽  
pp. 3793-3801 ◽  
Author(s):  
Latesh Lad ◽  
Jonathan Friedman ◽  
Huying Li ◽  
B. Bhaskar ◽  
Paul R. Ortiz de Montellano ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1

Binding mode of thiocyanate in palladium(II) complexes: x-ray crystal structure of cis-(isothiocyanato)(thiocyanato)bis(1-phenyl-3,4-dimethylphosphole)palladium(II)

1982 ◽  
Vol 21 (3) ◽  
pp. 1200-1204 ◽  
Author(s):  
John H. Nelson ◽  
J. Jeffrey. MacDougall ◽  
Nathaniel W. Alcock ◽  
Francois. Mathey
Keyword(s):  
Crystal Structure ◽  
Binding Mode ◽  
X Ray

scholarly journals Crystal Structure of Rat Heme Oxygenase-1 in Complex with Biliverdin-Iron Chelate

2003 ◽  
Vol 278 (34) ◽  
pp. 32352-32358 ◽  
Author(s):  
Masakazu Sugishima ◽  
Hiroshi Sakamoto ◽  
Yuichiro Higashimoto ◽  
Masato Noguchi ◽  
Keiichi Fukuyama
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Iron Chelate

Crystal Structure of Heme Oxygenase from the Gram-Negative PathogenNeisseria meningitidisand a Comparison with Mammalian Heme Oxygenase-1†

Biochemistry ◽  
2001 ◽  
Vol 40 (38) ◽  
pp. 11552-11558 ◽  
Author(s):  
David J. Schuller ◽  
Wenming Zhu ◽  
Igor Stojiljkovic ◽  
Angela Wilks ◽  
Thomas L. Poulos
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Gram Negative
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