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A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria

Author

Listed:
  • Nicolas Grosjean

    (Brookhaven National Laboratory
    Lawrence Berkeley National Laboratory)

  • Estella F. Yee

    (Brookhaven National Laboratory)

  • Desigan Kumaran

    (Brookhaven National Laboratory)

  • Kriti Chopra

    (Brookhaven National Laboratory)

  • Macon Abernathy

    (SLAC National Accelerator Laboratory)

  • Sandeep Biswas

    (Washington University)

  • James Byrnes

    (Brookhaven National Laboratory)

  • Dale F. Kreitler

    (Brookhaven National Laboratory)

  • Jan-Fang Cheng

    (Lawrence Berkeley National Laboratory)

  • Agnidipta Ghosh

    (Albert Einstein College of Medicine)

  • Steven C. Almo

    (Albert Einstein College of Medicine)

  • Masakazu Iwai

    (University of California
    Lawrence Berkeley National Laboratory)

  • Krishna K. Niyogi

    (University of California
    Lawrence Berkeley National Laboratory
    University of California)

  • Himadri B. Pakrasi

    (Washington University)

  • Ritimukta Sarangi

    (SLAC National Accelerator Laboratory)

  • Hubertus Dam

    (Brookhaven National Laboratory)

  • Lin Yang

    (Brookhaven National Laboratory)

  • Ian K. Blaby

    (Lawrence Berkeley National Laboratory
    Lawrence Berkeley National Laboratory)

  • Crysten E. Blaby-Haas

    (Brookhaven National Laboratory
    Lawrence Berkeley National Laboratory
    Lawrence Berkeley National Laboratory)

Abstract

Heme has a critical role in the chemical framework of the cell as an essential protein cofactor and signaling molecule that controls diverse processes and molecular interactions. Using a phylogenomics-based approach and complementary structural techniques, we identify a family of dimeric hemoproteins comprising a domain of unknown function DUF2470. The heme iron is axially coordinated by two zinc-bound histidine residues, forming a distinct two-fold symmetric zinc-histidine-iron-histidine-zinc site. Together with structure-guided in vitro and in vivo experiments, we further demonstrate the existence of a functional link between heme binding by Dri1 (Domain related to iron 1, formerly ssr1698) and post-translational regulation of succinate dehydrogenase in the cyanobacterium Synechocystis, suggesting an iron-dependent regulatory link between photosynthesis and respiration. Given the ubiquity of proteins containing homologous domains and connections to heme metabolism across eukaryotes and prokaryotes, we propose that DRI (Domain Related to Iron; formerly DUF2470) functions at the molecular level as a heme-dependent regulatory domain.

Suggested Citation

  • Nicolas Grosjean & Estella F. Yee & Desigan Kumaran & Kriti Chopra & Macon Abernathy & Sandeep Biswas & James Byrnes & Dale F. Kreitler & Jan-Fang Cheng & Agnidipta Ghosh & Steven C. Almo & Masakazu I, 2024. "A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47486-z
    DOI: 10.1038/s41467-024-47486-z
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    References listed on IDEAS

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    1. Alessandro Tagliabue & Andrew R. Bowie & Philip W. Boyd & Kristen N. Buck & Kenneth S. Johnson & Mak A. Saito, 2017. "The integral role of iron in ocean biogeochemistry," Nature, Nature, vol. 543(7643), pages 51-59, March.
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