Evidence map›Paper›PMID 30040901›Full record

ArticleJournal of chemical theory and computation2018

Accurate Quantum Mechanical/Molecular Mechanical Calculations of Reduction Potentials in Azurin Variants.

Lin Shen, Xiancheng Zeng, Hao Hu, Xiangqian Hu, Weitao Yang

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In one paragraph

Article in Journal of chemical theory and computation, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

3 citing papers in PubMed, 26 citations in OpenAlex.

  1. Theoretical Modeling of Redox Potentials of Biomolecules.Molecules (Basel, Switzerland) · 2022
    Review
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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

5 authors at 1 institution in 1 country.

Lin ShenDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Xiancheng ZengDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Hao HuDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Xiangqian HuDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Weitao YangDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.ORCID http://orcid.org/0000-0001-5576-2828
Duke University · US

Funding

COMPUTER SIMULATIONS OF ENZYMES AND DNAR01GM061870 · NIGMS · DUKE UNIVERSITY · PI YANG, WEITAO · 2000 to 2022
$5.5M
NIGMS NIH HHS R01 GM061870
6 · The paper itself

Abstract

Understanding the regulation mechanism and molecular determinants of the reduction potential of metalloprotein is a major challenge. An ab initio quantum mechanical/molecular mechanical (QM/MM) method combining the minimum free energy path (MFEP) and fractional number of electron (FNE) approaches has been developed in our group to simulate the redox processes of large systems. The FNE scheme provides an efficient unique description for the redox process, while the MFEP method provides improved conformational sampling on complex environments such as protein in the QM/MM calculations. The reduction potentials of wild-type and seven mutants of azurin, a type 1 copper metalloprotein, were simulated with the QM/MM-MFEP+FNE approach in this paper. A range of 350 mV for the variations of the reduction potentials of these azurin proteins was reproduced faithfully with relative errors around 20 mV. The correlation between structural interactions and reduction potentials observed in simulations provides in-depth insight into the regulation of reduction potentials, which potentially can also be very useful to the engineering of metalloprotein-based electrocatalysts in artificial photosynthesis. The excellent accuracy and efficiency of the QM/MM-MFEP+FNE approach demonstrate the potential for simulations of many electron transfer processes in condensed phases and biochemical systems.

Indexed as

Quantum TheoryAzurinCatalytic DomainCrystallography, X-RayMolecular ConformationMutationOxidation-ReductionPseudomonas aeruginosaAzurin

Identifiers

PMID30040901
PMCPMC6195766
OpenAlexW2883119021

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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.