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 ◽  
...  
2020 ◽  
Vol 477 (24) ◽  
pp. 4785-4796
Author(s):  
Jia Wang ◽  
Qi Guo ◽  
Xiaoyi Li ◽  
Xiao Wang ◽  
Lin Liu

Plant tetrapyrroles, including heme and bilins, are synthesized in plastids. Heme oxygenase (HO) catalyzes the oxidative cleavage of heme to the linear tetrapyrrole biliverdin as the initial step in bilin biosynthesis. Besides the canonical α-helical HO that is conserved from prokaryotes to human, a subfamily of non-canonical dimeric β-barrel HO has been found in bacteria. In this work, we discovered that the Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein that is structurally related to the putative non-canonical HO and is located in chloroplasts. The recombinant protein was able to bind and degrade heme in a manner different from known HO proteins. Crystal structure of the heme–protein complex reveals that the heme-binding site is in the interdimer interface and the heme iron is co-ordinated by a fixed water molecule. Our results identify a new protein that may function additionally in the tetrapyrrole biosynthetic pathway.


Biochemistry ◽  
1995 ◽  
Vol 34 (41) ◽  
pp. 13407-13411 ◽  
Author(s):  
Stephan Immenschuh ◽  
Shin-ichiro Iwahara ◽  
Hiroyuki Satoh ◽  
Christina Nell ◽  
Norbert Katz ◽  
...  

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

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

2003 ◽  
Vol 278 (34) ◽  
pp. 32352-32358 ◽  
Author(s):  
Masakazu Sugishima ◽  
Hiroshi Sakamoto ◽  
Yuichiro Higashimoto ◽  
Masato Noguchi ◽  
Keiichi Fukuyama

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

Biochemistry ◽  
2001 ◽  
Vol 40 (38) ◽  
pp. 11552-11558 ◽  
Author(s):  
David J. Schuller ◽  
Wenming Zhu ◽  
Igor Stojiljkovic ◽  
Angela Wilks ◽  
Thomas L. Poulos

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