Evidence map›Paper›PMID 33597529›Full record

ArticleNature communications2021

Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c.

Marco E Reinhard, Michael W Mara, Thomas Kroll, Hyeongtaek Lim, Ryan G Hadt, Roberto Alonso-Mori, Matthieu Chollet, James M Glownia, Silke Nelson, Dimosthenis Sokaras and 12 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

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  6. Stimulated X-ray emission spectroscopy.Photosynthesis research · 2024
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  9. The role of basicity in selective C-H bond activation by transition metal-oxidos.Dalton transactions (Cambridge, England : 2003) · 2023
    Review
  10. Article
  11. Reaction dynamics studiedChemical science · 2022
    Review
  12. Review
  13. Review
  14. 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

22 authors at 4 institutions in 1 country.

Marco E ReinhardPULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
Michael W MaraDepartment of Chemistry, Stanford University, Stanford, CA, USA.
Thomas KrollStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Hyeongtaek LimDepartment of Chemistry, Stanford University, Stanford, CA, USA.ORCID 0000-0003-3470-8296
Ryan G HadtDepartment of Chemistry, Stanford University, Stanford, CA, USA.ORCID 0000-0001-6026-1358
Roberto Alonso-MoriLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.ORCID 0000-0002-5357-0934
Matthieu CholletLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
James M GlowniaLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Silke NelsonLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Dimosthenis SokarasStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Kristjan KunnusPULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
Tim Brandt van DrielLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Robert W HartsockPULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
Kasper S KjaerPULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
Clemens WeningerLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Elisa BiasinPULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.ORCID 0000-0002-7276-4224
Leland B GeeDepartment of Chemistry, Stanford University, Stanford, CA, USA.
Keith O HodgsonStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Britt HedmanStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Uwe BergmannPULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.ORCID 0000-0001-5639-166X
Edward I SolomonStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA. edward.solomon@stanford.edu.ORCID 0000-0003-0291-3199
Kelly J GaffneyPULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA. kgaffney@slac.stanford.edu.ORCID 0000-0002-0525-6465
SLAC National Accelerator Laboratory · USStanford University · USCalifornia Institute of Technology · USNorthwestern University · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
SPECTROSCOPIC STUDIES OF NONHEME IRON ENZYMESR01GM040392 · NIGMS · STANFORD UNIVERSITY · PI SOLOMON, EDWARD I · 1988 to 2021
$8.6M
Electronic Structure of Heme Enzyme Intermediates from Resonant Inelastic X-ray Scattering and L-Edge X-ray Absorption SpectroscopyF32GM122194 · NIGMS · STANFORD UNIVERSITY · PI GEE, LELAND BRUCE · 2017 to 2020
$227k
NIGMS NIH HHS F32 GM122194NIGMS NIH HHS P41 GM103393
6 · The paper itself

Abstract

The dynamics of photodissociation and recombination in heme proteins represent an archetypical photochemical reaction widely used to understand the interplay between chemical dynamics and reaction environment. We report a study of the photodissociation mechanism for the Fe(II)-S bond between the heme iron and methionine sulfur of ferrous cytochrome c. This bond dissociation is an essential step in the conversion of cytochrome c from an electron transfer protein to a peroxidase enzyme. We use ultrafast X-ray solution scattering to follow the dynamics of Fe(II)-S bond dissociation and 1s3p (Kβ) X-ray emission spectroscopy to follow the dynamics of the iron charge and spin multiplicity during bond dissociation. From these measurements, we conclude that the formation of a triplet metal-centered excited state with anti-bonding Fe(II)-S interactions triggers the bond dissociation and precedes the formation of the metastable Fe high-spin quintet state.

Indexed as

Cytochromes cElectron TransportFerrous CompoundsHemeIronMetalsMethionineMolecular Dynamics SimulationPhotolysisSpectrometry, X-Ray EmissionCytochromes cFerrous CompoundsHemeIronMetalsMethionine

Identifiers

PMID33597529
PMCPMC7889893
OpenAlexW3131969473

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.