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From Synthesis to Utilization: The Ins and Outs of Mitochondrial Heme

Samantha A. Swenson, Courtney M. Moore, Jason R. Marcero, Amy E. Medlock, Amit R. Reddi, Oleh Khalimonchuk

Cells. 2020 Mar; 9(3): 579. Published online 2020 Feb 29. doi: 10.3390/cells9030579

PMCID:: PMC7140478

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Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells

David A. Hanna, Courtney M. Moore, Liu Liu, Xiaojing Yuan, Iramofu M. Dominic, Angela S. Fleischhacker, Iqbal Hamza, Stephen W. Ragsdale, Amit R. Reddi

J Biol Chem. 2022 Feb; 298(2): 101549. Published online 2021 Dec 29. doi: 10.1016/j.jbc.2021.101549

PMCID:: PMC8808069

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Regulation of protein function and degradation by heme, heme responsive motifs, and CO

Angela S. Fleischhacker, Anindita Sarkar, Liu Liu, Stephen W. Ragsdale

Crit Rev Biochem Mol Biol. Author manuscript; available in PMC 2023 Feb 1.

Published in final edited form as: Crit Rev Biochem Mol Biol. 2022 Feb; 57(1): 16–47. Published online 2021 Sep 13. doi: 10.1080/10409238.2021.1961674

PMCID:: PMC8966953

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Mitochondrial contact site and cristae organizing system (MICOS) machinery supports heme biosynthesis by enabling optimal performance of ferrochelatase

Jonathan V. Dietz, Mathilda M. Willoughby, Robert B. Piel, III, Teresa A. Ross, Iryna Bohovych, Hannah G. Addis, Jennifer L. Fox, William N. Lanzilotta, Harry A. Dailey, James A. Wohlschlegel, Amit R. Reddi, Amy E. Medlock, Oleh Khalimonchuk

Redox Biol. 2021 Oct; 46: 102125. Published online 2021 Sep 10. doi: 10.1016/j.redox.2021.102125

PMCID:: PMC8441213

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Heme acquisition in the parasitic filarial nematode Brugia malayi

Ashley N. Luck, Xiaojing Yuan, Denis Voronin, Barton E. Slatko, Iqbal Hamza, Jeremy M. Foster

FASEB J. 2016 Oct; 30(10): 3501–3514. Published online 2016 Jun 30. doi: 10.1096/fj.201600603R

PMCID:: PMC5024691

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Biosynthesis and trafficking of heme o and heme a: New structural insights and their implications for reaction mechanisms and prenylated heme transfer

Elise D. Rivett, Lim Heo, Michael Feig, Eric L. Hegg

Crit Rev Biochem Mol Biol. Author manuscript; available in PMC 2022 Feb 25.

Published in final edited form as: Crit Rev Biochem Mol Biol. 2021 Dec; 56(6): 640–668. Published online 2021 Aug 25. doi: 10.1080/10409238.2021.1957668

PMCID:: PMC8877297

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Heme Synthesis and Acquisition in Bacterial Pathogens

Jacob E. Choby, Eric P. Skaar

J Mol Biol. Author manuscript; available in PMC 2016 Nov 28.

Published in final edited form as: J Mol Biol. 2016 Aug 28; 428(17): 3408–3428. Published online 2016 Mar 24. doi: 10.1016/j.jmb.2016.03.018

PMCID:: PMC5125930

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Transcriptomic analyses of Aedes aegypti cultured cells and ex vivo midguts in response to an excess or deficiency of heme: a quest for transcriptionally-regulated heme transporters

Heather Eggleston, Zach N. Adelman

BMC Genomics. 2020; 21: 604. Published online 2020 Aug 31. doi: 10.1186/s12864-020-06981-5

PMCID:: PMC7460771

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Handling heme: The mechanisms underlying the movement of heme within and between cells

Rebecca K. Donegan, Courtney M. Moore, David A. Hanna, Amit R. Reddi

Free Radic Biol Med. Author manuscript; available in PMC 2020 Mar 1.

Published in final edited form as: Free Radic Biol Med. 2019 Mar; 133: 88–100. Published online 2018 Aug 6. doi: 10.1016/j.freeradbiomed.2018.08.005

PMCID:: PMC6363905

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One ring to bring them all and in the darkness bind them: The Trafficking of Heme without Deliverers.

Ian G. Chambers, Mathilda M. Willoughby, Iqbal Hamza, Amit R. Reddi

Biochim Biophys Acta Mol Cell Res. Author manuscript; available in PMC 2022 Jan 1.

Published in final edited form as: Biochim Biophys Acta Mol Cell Res. 2021 Jan; 1868(1): 118881. Published online 2020 Oct 3. doi: 10.1016/j.bbamcr.2020.118881

PMCID:: PMC7756907

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Significance of Heme and Heme Degradation in the Pathogenesis of Acute Lung and Inflammatory Disorders

Stefan W. Ryter

Int J Mol Sci. 2021 Jun; 22(11): 5509. Published online 2021 May 24. doi: 10.3390/ijms22115509

PMCID:: PMC8197128

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Unravelling the mechanisms controlling heme supply and demand

Galvin C.-H. Leung, Simon S.-P. Fung, Andrea E. Gallio, Robert Blore, Dominic Alibhai, Emma L. Raven, Andrew J. Hudson

Proc Natl Acad Sci U S A. 2021 Jun 1; 118(22): e2104008118. Published online 2021 May 25. doi: 10.1073/pnas.2104008118

PMCID:: PMC8179208

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

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

J Biol Chem. 2020 Apr 17; 295(16): 5177–5191. Published online 2020 Mar 9. doi: 10.1074/jbc.RA120.012803

PMCID:: PMC7170523

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Regulation of intracellular heme trafficking revealed by subcellular reporters

Xiaojing Yuan, Nicole Rietzschel, Hanna Kwon, Ana Beatriz Walter Nuno, David A. Hanna, John D. Phillips, Emma L. Raven, Amit R. Reddi, Iqbal Hamza

Proc Natl Acad Sci U S A. 2016 Aug 30; 113(35): E5144–E5152. Published online 2016 Aug 15. doi: 10.1073/pnas.1609865113

PMCID:: PMC5024633

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Redox Regulation of Heme Oxygenase-2 and the Transcription Factor, Rev-Erb, Through Heme Regulatory Motifs

Angela S. Fleischhacker, Eric L. Carter, Stephen W. Ragsdale

Antioxid Redox Signal. 2018 Dec 20; 29(18): 1841–1857. Published online 2018 Nov 1. doi: 10.1089/ars.2017.7368

PMCID:: PMC6217750

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Heme bioavailability and signaling in response to stress in yeast cells

David A. Hanna, Rebecca Hu, Hyojung Kim, Osiris Martinez-Guzman, Matthew P. Torres, Amit R. Reddi

J Biol Chem. 2018 Aug 10; 293(32): 12378–12393. Published online 2018 Jun 19. doi: 10.1074/jbc.RA118.002125

PMCID:: PMC6093230

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Heme Detoxification in the Malaria Parasite: A Target for Antimalarial Drug Development

Katherine A. de Villiers, Timothy J. Egan

Acc Chem Res. Author manuscript; available in PMC 2022 Jun 1.

Published in final edited form as: Acc Chem Res. 2021 Jun 1; 54(11): 2649–2659. Published online 2021 May 13. doi: 10.1021/acs.accounts.1c00154

PMCID:: PMC8290263

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Molecular Mechanisms of Iron and Heme Metabolism

Sohini Dutt, Iqbal Hamza, Thomas Benedict Bartnikas

Annu Rev Nutr. Author manuscript; available in PMC 2022 Dec 22.

Published in final edited form as: Annu Rev Nutr. 2022 Aug 22; 42: 311–335. Published online 2022 May 4. doi: 10.1146/annurev-nutr-062320-112625

PMCID:: PMC9398995

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Heme Oxygenase 1: A Defensive Mediator in Kidney Diseases

Anne Grunenwald, Lubka T. Roumenina, Marie Frimat

Int J Mol Sci. 2021 Feb; 22(4): 2009. Published online 2021 Feb 18. doi: 10.3390/ijms22042009

PMCID:: PMC7923026

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GAPDH is involved in the heme-maturation of myoglobin and hemoglobin

Blair Tupta, Eric Stuehr, Mamta P. Sumi, Elizabeth A. Sweeny, Brandon Smith, Dennis J. Stuehr, Arnab Ghosh

FASEB J. Author manuscript; available in PMC 2022 Jun 28.

Published in final edited form as: FASEB J. 2022 Feb; 36(2): e22099. doi: 10.1096/fj.202101237RR

PMCID:: PMC9239731

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PMC Images search for ferroprotoporphyrin

FIG. 2.

Amino acid substitution of Leu29 with phenylalanine increases O₂ affinity. Phenylalanine at site B10 stabilizes O₂ that is liganded to the iron atom of ferroprotoporphyrin IX in Mb. L29F is used to describe this Mb mutant because site B10 is the 29th residue in sperm whale Mb. Leucine at B10 in native Mb does not stabilize O₂ to the iron atom of ferroprotoporphyrin IX, which results in lower O₂ affinity. Image is adapted from ref. ().

Redox Reactions of Myoglobin

Antioxid Redox Signal. 2013 Jun 10;18(17):2342-2351.
Figure 10

Digestion of hemoglobin (27) to give ferroprotoporphyrin (28), which spontaneously oxidizes to ferriprotoporphyrin IX (29). Precipitation of hemozoin (30) prevents the toxic effects of 29 [,].

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Biomedicines. 2021 May;9(5):472.
FIG. 1.

Heme degradation by heme oxygenase. The catabolism of heme (ferroprotoporphyrin IX) via heme oxygenase requires the participation of NADPH and O₂. Heme is broken and oxidized at the α-methene bridge, producing equimolar amounts of CO, ferrous iron, and biliverdin. From Wu and Wang ref. .

Heme Degradation and Vascular Injury

Antioxid Redox Signal. 2010 Jan 15;12(2):233-248.
Scheme 4

The iron(II) ion of ferroprotoporphyrin (27) activates artemisinin (31) to give a reactive C-radical (36), which might alkylate ferroporotporphyrin (27) preventing precipitation []. The exact mechanism of alkylation, C-radial formation and the possibility of degradation of other biomolecules are still debated [].

Natural Products That Changed Society

Biomedicines. 2021 May;9(5):472.