Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures.
Enzymatic reaction
Heme metabolism
Ligand discrimination
Protein structure
Redox complex
Stacked substrate-binding mode
X-ray crystallography.
Journal
Current medicinal chemistry
ISSN: 1875-533X
Titre abrégé: Curr Med Chem
Pays: United Arab Emirates
ID NLM: 9440157
Informations de publication
Date de publication:
2020
2020
Historique:
received:
28
08
2018
revised:
21
11
2018
accepted:
11
12
2018
pubmed:
18
12
2018
medline:
13
8
2020
entrez:
18
12
2018
Statut:
ppublish
Résumé
In mammals, catabolism of the heme group is indispensable for life. Heme is first cleaved by the enzyme Heme Oxygenase (HO) to the linear tetrapyrrole Biliverdin IXα (BV), and BV is then converted into bilirubin by Biliverdin Reductase (BVR). HO utilizes three Oxygen molecules (O2) and seven electrons supplied by NADPH-cytochrome P450 oxidoreductase (CPR) to open the heme ring and BVR reduces BV through the use of NAD(P)H. Structural studies of HOs, including substrate-bound, reaction intermediate-bound, and several specific inhibitor-bound forms, reveal details explaining substrate binding to HO and mechanisms underlying-specific HO reaction progression. Cryo-trapped structures and a time-resolved spectroscopic study examining photolysis of the bond between the distal ligand and heme iron demonstrate how CO, produced during the HO reaction, dissociates from the reaction site with a corresponding conformational change in HO. The complex structure containing HO and CPR provides details of how electrons are transferred to the heme-HO complex. Although the tertiary structure of BVR and its complex with NAD+ was determined more than 10 years ago, the catalytic residues and the reaction mechanism of BVR remain unknown. A recent crystallographic study examining cyanobacterial BVR in complex with NADP+ and substrate BV provided some clarification regarding these issues. Two BV molecules are bound to BVR in a stacked manner, and one BV may assist in the reductive catalysis of the other BV. In this review, recent advances illustrated by biochemical, spectroscopic, and crystallographic studies detailing the chemistry underlying the molecular mechanism of HO and BVR reactions are presented.
Identifiants
pubmed: 30556496
pii: CMC-EPUB-95280
doi: 10.2174/0929867326666181217142715
pmc: PMC7509768
doi:
Substances chimiques
Heme
42VZT0U6YR
Heme Oxygenase (Decyclizing)
EC 1.14.14.18
Oxidoreductases Acting on CH-CH Group Donors
EC 1.3.-
biliverdin reductase
EC 1.3.1.24
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
3499-3518Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM118217
Pays : United States
Informations de copyright
Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.
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