Evidence map›Paper›PMID 38609367›Full record

ArticleNature communications2024

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

Nicolas Grosjean, Estella F Yee, Desigan Kumaran, Kriti Chopra, Macon Abernathy, Sandeep Biswas, James Byrnes, Dale F Kreitler, Jan-Fang Cheng, Agnidipta Ghosh and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Rv3839-Rv3840 links the endogenous heme biosynthesis pathway withbioRxiv : the preprint server for biology · 2026
    Article
  3. Metabolic engineering ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors at 6 institutions in 1 country.

Nicolas GrosjeanBiology Department, Brookhaven National Laboratory, Upton, NY, USA.ORCID http://orcid.org/0000-0002-8146-7862
Estella F YeeNational Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY, USA.ORCID http://orcid.org/0000-0001-7108-1387
Desigan KumaranBiology Department, Brookhaven National Laboratory, Upton, NY, USA.
Kriti ChopraComputational Science Initiative, Brookhaven National Laboratory, Upton, NY, USA.ORCID http://orcid.org/0000-0002-9788-9218
Macon AbernathyStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
Sandeep BiswasDepartment of Biology, Washington University, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-9718-8948
James ByrnesNational Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY, USA.
Dale F KreitlerNational Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY, USA.
Jan-Fang ChengUS Department of Energy Joint Genome Institute, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0001-7315-7613
Agnidipta GhoshDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA.ORCID http://orcid.org/0000-0002-7753-0240
Steven C AlmoDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA.
Masakazu IwaiDepartment of Plant and Microbial Biology, University of California, Berkeley, CA, USA.
Krishna K NiyogiDepartment of Plant and Microbial Biology, University of California, Berkeley, CA, USA.ORCID http://orcid.org/0000-0001-7229-2071
Himadri B PakrasiDepartment of Biology, Washington University, St. Louis, MO, USA.ORCID http://orcid.org/0000-0001-8240-2123
Ritimukta SarangiStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.ORCID http://orcid.org/0000-0002-2764-2279
Hubertus van DamCondensed Matter Physics and Materials Science Department, Brookhaven National Laboratory, Upton, NY, USA.ORCID http://orcid.org/0000-0002-0876-3294
Lin YangNational Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY, USA.ORCID http://orcid.org/0000-0003-1057-9194
Ian K BlabyUS Department of Energy Joint Genome Institute, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-1631-3154
Crysten E Blaby-HaasBiology Department, Brookhaven National Laboratory, Upton, NY, USA. cblaby@lbl.gov.ORCID http://orcid.org/0000-0002-1583-1291
Brookhaven National Laboratory · USLawrence Berkeley National Laboratory · USAlbert Einstein College of Medicine · USSLAC National Accelerator Laboratory · USWashington University in St. Louis · USHoward Hughes Medical Institute · US

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
National Biomedical Resource for Electron-Spin Resonance Spectroscopy (ACERT)R24GM146107 · NIGMS · CORNELL UNIVERSITY · PI BRIAN R CRANE, Jack H Freed · 2022 to 2026
$6.4M
National HTX Center: Enabling Access to State-of-the-Art Crystallization CapabilitiesR24GM141256 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI Sarah Elizabeth Johnson Bowman · 2021 to 2026
$6.3M
NIGMS NIH HHS P30 GM133893NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R24 GM141256NIGMS NIH HHS R24 GM146107
6 · The paper itself

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.

Indexed as

HemeproteinsSynechocystisCarbonHemeHistidineIronZincCarbonHemeHemeproteinsHistidineIronZinc

Identifiers

PMID38609367
PMCPMC11014987
OpenAlexW4394757848

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.