دورية أكاديمية
أعرض في EDS

A noncanonical heme oxygenase specific for the degradation of c-type heme.

التفاصيل البيبلوغرافية
العنوان: A noncanonical heme oxygenase specific for the degradation of c-type heme.
المؤلفون: Li S; Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama, USA., Isiorho EA; Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama, USA., Owens VL; Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama, USA., Donnan PH; Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama, USA., Odili CL; Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama, USA., Mansoorabadi SO; Department of Chemistry and Biochemistry, Auburn University, Auburn, Alabama, USA. Electronic address: som@auburn.edu.
المصدر: The Journal of biological chemistry [J Biol Chem] 2021 Jan-Jun; Vol. 296, pp. 100666. Date of Electronic Publication: 2021 Apr 17.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
مواضيع طبية MeSH: Bacterial Proteins/*metabolism , Biliverdine/*metabolism , Heme/*analogs & derivatives , Heme/*metabolism , Heme Oxygenase (Decyclizing)/*metabolism , Iron/*metabolism , Membrane Transport Proteins/*metabolism , Paracoccus denitrificans/*enzymology, Catalysis ; Crystallography, X-Ray ; Heme Oxygenase (Decyclizing)/chemistry ; Substrate Specificity
مستخلص: Heme oxygenases (HOs) play a critical role in recouping iron from the labile heme pool. The acquisition and liberation of heme iron are especially important for the survival of pathogenic bacteria. All characterized HOs, including those belonging to the HugZ superfamily, preferentially cleave free b-type heme. Another common form of heme found in nature is c-type heme, which is covalently linked to proteinaceous cysteine residues. However, mechanisms for direct iron acquisition from the c-type heme pool are unknown. Here we identify a HugZ homolog from the oligopeptide permease (opp) gene cluster of Paracoccus denitrificans that lacks any observable reactivity with heme b and show that it instead rapidly degrades c-type hemopeptides. This c-type heme oxygenase catalyzes the oxidative cleavage of the model substrate microperoxidase-11 at the β- and/or δ-meso position(s), yielding the corresponding peptide-linked biliverdin, CO, and free iron. X-ray crystallographic analysis suggests that the switch in substrate specificity from b-to c-type heme involves loss of the N-terminal α/β domain and C-terminal loop containing the coordinating histidine residue characteristic of HugZ homologs, thereby accommodating a larger substrate that provides its own iron ligand. These structural features are also absent in certain heme utilization/storage proteins from human pathogens that exhibit low or no HO activity with free heme. This study thus expands the scope of known iron acquisition strategies to include direct oxidative cleavage of heme-containing proteolytic fragments of c-type cytochromes and helps to explain why certain oligopeptide permeases show specificity for the import of heme in addition to peptides.
Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
(Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)
References: Biochim Biophys Acta Gen Subj. 2017 Jul;1861(7):1870-1878. (PMID: 28385652)
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42. (PMID: 21460441)
Chem Commun (Camb). 2012 Jul 7;48(53):6741-3. (PMID: 22627893)
Prz Gastroenterol. 2014;9(4):208-13. (PMID: 25276251)
Biometals. 2016 Aug;29(4):593-609. (PMID: 27154580)
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2184-95. (PMID: 15572771)
BMC Struct Biol. 2012 Sep 26;12:23. (PMID: 23013214)
World J Gastroenterol. 2008 Jul 14;14(26):4101-10. (PMID: 18636652)
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. (PMID: 19461840)
Arch Biochem Biophys. 2014 Feb 15;544:87-95. (PMID: 24161941)
BMC Bioinformatics. 2016 Apr 18;17:168. (PMID: 27089923)
J Inorg Biochem. 2016 Jan;154:103-13. (PMID: 26598215)
J Biol Chem. 1969 Dec 10;244(23):6388-94. (PMID: 4390967)
J Biol Chem. 2005 Jan 28;280(4):2840-6. (PMID: 15520015)
Proc Natl Acad Sci U S A. 1968 Oct;61(2):748-55. (PMID: 4386763)
Methods Enzymol. 1997;276:307-26. (PMID: 27754618)
Biochim Biophys Acta. 1991 May 23;1058(1):17-20. (PMID: 1646010)
Nutrients. 2014 Mar 13;6(3):1080-102. (PMID: 24633395)
Nat Prod Rep. 2008 Dec;25(6):1118-30. (PMID: 19030605)
J Bacteriol. 1997 Feb;179(3):838-45. (PMID: 9006041)
J Bacteriol. 2000 Dec;182(23):6783-90. (PMID: 11073924)
Nat Protoc. 2008;3(7):1171-9. (PMID: 18600222)
Dalton Trans. 2017 Jun 27;46(25):8104-8109. (PMID: 28607990)
FEBS Lett. 2000 Apr 7;471(1):61-6. (PMID: 10760513)
IUCrJ. 2014 May 30;1(Pt 4):213-20. (PMID: 25075342)
J Biol Chem. 2013 Apr 5;288(14):10101-10109. (PMID: 23420845)
Biochemistry. 2013 May 7;52(18):3025-7. (PMID: 23600533)
Microbiol Mol Biol Rev. 1998 Dec;62(4):1046-78. (PMID: 9841665)
BMC Microbiol. 2008 Dec 17;8:226. (PMID: 19091096)
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501. (PMID: 20383002)
Experientia. 1968 Mar 15;24(3):219-21. (PMID: 5661404)
Front Cell Infect Microbiol. 2018 Jun 19;8:198. (PMID: 29971218)
J Biol Chem. 2019 Jan 18;294(3):1070-1082. (PMID: 30455346)
Arch Biochem Biophys. 2009 Jan 1;481(1):1-15. (PMID: 18977196)
FEMS Microbiol Rev. 2003 Jun;27(2-3):215-37. (PMID: 12829269)
Antioxid Redox Signal. 2004 Oct;6(5):825-34. (PMID: 15345142)
J Biol Chem. 1982 Sep 10;257(17):9944-52. (PMID: 6809753)
Mol Microbiol. 2010 Mar;75(6):1529-38. (PMID: 20180905)
FEBS Lett. 2016 Dec;590(23):4393-4401. (PMID: 27714801)
Trends Mol Med. 2016 Dec;22(12):1077-1090. (PMID: 27825668)
J Bacteriol. 2001 Nov;183(21):6394-403. (PMID: 11591684)
Annu Rev Microbiol. 2000;54:881-941. (PMID: 11018148)
J Biol Chem. 2011 Jan 14;286(2):1537-44. (PMID: 21030596)
Biochemistry. 2017 May 30;56(21):2723-2734. (PMID: 28481076)
J Mol Biol. 2015 Nov 6;427(22):3554-3571. (PMID: 26434506)
Res Microbiol. 2019 Nov - Dec;170(8):338-344. (PMID: 31376485)
J Biol Chem. 1982 Jul 10;257(13):7803-7. (PMID: 6806285)
J Biol Chem. 2006 Oct 27;281(43):32606-10. (PMID: 16943192)
Amino Acids. 2013 May;44(5):1267-77. (PMID: 23443998)
Molecules. 2021 Jan 21;26(3):. (PMID: 33494451)
معلومات مُعتمدة: P30 GM138396 United States GM NIGMS NIH HHS; S10 OD012289 United States OD NIH HHS
فهرسة مساهمة: Keywords: c-type heme; heme oxygenase; iron metabolism; peptide transport; structure–function
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Membrane Transport Proteins)
26598-29-8 (heme C)
39335-07-4 (oligopeptide permease, Bacteria)
42VZT0U6YR (Heme)
E1UOL152H7 (Iron)
EC 1.14.14.18 (Heme Oxygenase (Decyclizing))
O9MIA842K9 (Biliverdine)
تواريخ الأحداث: Date Created: 20210416 Date Completed: 20210823 Latest Revision: 20210823
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC8131568
DOI: 10.1016/j.jbc.2021.100666
PMID: 33862082
قاعدة البيانات: MEDLINE
الوصف
تدمد:1083-351X
DOI:10.1016/j.jbc.2021.100666