Biochemical and Biophysical Research Communications
Volume 157, Issue 2, 15 December 1988, Pages 480-487
Properties of human kidney heme oxygenase: Inhibition by synthetic heme analogues and metalloporphyrins
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2011, Archives of Biochemistry and BiophysicsCitation Excerpt :Heme oxygenase-1 (HO-1) is the CYPOR-dependent, stress-inducible, membrane-bound enzyme that breaks heme down to carbon monoxide (CO), ferrous iron (Fe2+), and biliverdin. Biliverdin is further degraded to bilirubin by the cytosolic enzyme biliverdin reductase (BVR) [24,25], in human spleen, liver, and kidney [26,27]. The C-terminal transmembrane segment of HO-1 was previously shown to drive high-affinity functional complexation with CYPOR [28] and was recently shown to be crucial for HO-1 oligomerization, thereby contributing to its stability and function [29].
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Copyright © 1988 Published by Elsevier Inc.