The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation-Reference-Cited by-同舟云学术

The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation

Published:2020-04 Issue:16 Volume:295 Page:5177-5191
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fleischhacker Angela S.^ORCID,Gunawan Amanda L.,Kochert Brent A.,Liu Liu^ORCID,Wales Thomas E.,Borowy Maelyn C.,Engen John R.^ORCID,Ragsdale Stephen W.^ORCID

Funder

HHS | NIH | National Institute of General Medical Sciences

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference47 articles.

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3. Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2;Bianchetti;J. Biol. Chem,2007

4. Heme binds to a short sequence that serves a regulatory function in diverse proteins;Zhang;EMBO J,1995

5. The C-terminal heme regulatory motifs of heme oxygenase-2 are redox-regulated heme binding sites;Fleischhacker;Biochemistry,2015

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