Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2

被引：52

作者：

Bianchetti, Christopher M. ^{[1
,2
,3
]}

Yi, Li ^{[4
]}

Ragsdale, Stephen W. ^{[4
]}

Phillips, George N., Jr. ^{[1
,3
]}

机构：

[1] Univ Wisconsin, Dept Biochem, 433 Babcock Dr, Madison, WI 53706 USA

[2] Univ Wisconsin, Grad Program Biophys, Madison, WI 53706 USA

[3] Univ Wisconsin, Ctr Eukaryot Struct Genom, Madison, WI 53706 USA

[4] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2007年 / 282卷 / 52期

关键词：

D O I：

10.1074/jbc.M707396200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal structures of apo-and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His(45), resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr(154), Lys(199), and Arg(203) orient the heme through direct interactions with the heme propionates. The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions.

引用

页码：37624 / 37631

页数：8

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