Evidence map›Paper›PMID 31001586›Full record

ArticleScience advances2019

A 192-heme electron transfer network in the hydrazine dehydrogenase complex.

M Akram, A Dietl, U Mersdorf, S Prinz, W Maalcke, J Keltjens, C Ferousi, N M de Almeida, J Reimann, B Kartal and 3 more

Abstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Lysine or histidine? examining the role of the proximal ligand at the active heme center of cytochrome c nitrite reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
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  6. Review
  7. Article
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  15. Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  16. Article
  17. Specificity of SmallACS omega · 2021
    Article
  18. Article
  19. Review
  20. Role of multiheme cytochromes involved in extracellular anaerobic respiration in bacteria.Protein science : a publication of the Protein Society · 2020
    Review
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

13 authors.

M AkramDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.ORCID 0000-0002-0765-239X
A DietlDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.
U MersdorfDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.
S PrinzDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.
W MaalckeDepartment of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands.ORCID 0000-0002-3736-7282
J KeltjensDepartment of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands.
C FerousiDepartment of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands.ORCID 0000-0001-6400-7373
N M de AlmeidaDepartment of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands.
J ReimannDepartment of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands.
B KartalDepartment of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands.
M S M JettenDepartment of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands.
K PareyDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.ORCID 0000-0002-4842-6479
T R M BarendsDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.ORCID 0000-0002-9488-3005

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas and water through the highly reactive intermediate hydrazine. So far, it is unknown how anammox organisms convert the toxic hydrazine into nitrogen and harvest the extremely low potential electrons (-750 mV) released in this process. We report the crystal structure and cryo electron microscopy structures of the responsible enzyme, hydrazine dehydrogenase, which is a 1.7 MDa multiprotein complex containing an extended electron transfer network of 192 heme groups spanning the entire complex. This unique molecular arrangement suggests a way in which the protein stores and releases the electrons obtained from hydrazine conversion, the final step in the globally important anammox process.

Indexed as

Bacterial ProteinsBinding SitesCatalytic DomainCryoelectron MicroscopyCrystallography, X-RayElectron TransportGram-Negative BacteriaHemeOxidoreductasesProtein Structure, QuaternaryBacterial ProteinsHemeOxidoreductases

Identifiers

PMID31001586
PMCPMC6469936

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Registered trials

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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.