ArticleJournal of biochemistry2016
Redox-coupled structural changes in nitrite reductase revealed by serial femtosecond and microfocus crystallography.
Article in Journal of biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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.
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.
Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Tracking Protein Motions using Serial Femtosecond Crystallography with X-Ray Free-Electron Laser.Current protocols · 2025Article
- Quantifying and comparing radiation damage in the Protein Data Bank.Nature communications · 2022Article
- Crystal structure of CmABCB1 multi-drug exporter in lipidic mesophase revealed by LCP-SFX.IUCrJ · 2022Article
- Copper nitrite reductase from Sinorhizobium meliloti 2011: Crystal structure and interaction with the physiological versus a nonmetabolically related cupredoxin-like mediator.Protein science : a publication of the Protein Society · 2021Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.Science advances · 2021Article
- High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Article
- Review
- Serial femtosecond crystallography at the SACLA: breakthrough to dynamic structural biology.Biophysical reviews · 2018Review
- Multi-wavelength anomalous diffraction de novo phasing using a two-colour X-ray free-electron laser with wide tunability.Nature communications · 2017Article
- Article
- Hydroxyethyl cellulose matrix applied to serial crystallography.Scientific reports · 2017Article
- Atomic resolution structure of serine protease proteinase K at ambient temperature.Scientific reports · 2017Article
- New molecular packing in a crystal of pseudoazurin from Alcaligenes faecalis: a double-helical arrangement of blue copper.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Membrane protein structure determination by SAD, SIR, or SIRAS phasing in serial femtosecond crystallography using an iododetergent.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
19 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serial femtosecond crystallography (SFX) has enabled the damage-free structural determination of metalloenzymes and filled the gaps of our knowledge between crystallographic and spectroscopic data. Crystallographers, however, scarcely know whether the rising technique provides truly new structural insights into mechanisms of metalloenzymes partly because of limited resolutions. Copper nitrite reductase (CuNiR), which converts nitrite to nitric oxide in denitrification, has been extensively studied by synchrotron radiation crystallography (SRX). Although catalytic Cu (Type 2 copper (T2Cu)) of CuNiR had been suspected to tolerate X-ray photoreduction, we here showed that T2Cu in the form free of nitrite is reduced and changes its coordination structure in SRX. Moreover, we determined the completely oxidized CuNiR structure at 1.43 Å resolution with SFX. Comparison between the high-resolution SFX and SRX data revealed the subtle structural change of a catalytic His residue by X-ray photoreduction. This finding, which SRX has failed to uncover, provides new insight into the reaction mechanism of CuNiR.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.