Evidence map›Paper›PMID 21322497›Full record

ArticleFaraday discussions2011

Engineering enzymes.

P Leslie Dutton, Christopher C Moser

Abstract read
In one paragraph

Article in Faraday discussions, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. The journal of physical chemistry. C, Nanomaterials and interfaces · 2025
    Article
  2. Review
  3. Review
  4. The ascent of man(made oxidoreductases).Current opinion in structural biology · 2018
    Review
  5. Review
  6. Synthetic beta-solenoid proteins with the fragment-free computational design of a beta-hairpin extension.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  7. Review
  8. Review
  9. Article
  10. Developments in the tools and methodologies of synthetic biology.Frontiers in bioengineering and biotechnology · 2014
    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

2 authors.

P Leslie DuttonJohnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA. dutton@mail.med.upenn.edu
Christopher C Moser

Funding

Natural Engineering of Multi-Electron Biological Oxidation & ReductionR01GM041048 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DUTTON, PETER LESLIE · 1989 to 2014
$5.0M
NIGMS NIH HHS GM 41048NIGMS NIH HHS R01 GM041048
6 · The paper itself

Abstract

Fundamental research into bioinorganic catalysis of the kind presented at this Faraday Discussion has the potential to turn inspiration drawn from impressive natural energy and chemical transformations into artificial catalyst constructions useful to mankind. Creating bio-inspired artificial constructions requires a level of understanding well beyond simple description of structures and mechanisms of natural enzymes. To be useful, such description must be augmented by a practical sense of structural and energetic engineering tolerances of the mechanism. Significant barriers to achieving an engineering understanding of enzyme mechanisms arise from natural protein complexity. In certain cases we can surmount these barriers to understanding, such as natural electron tunneling, coupling of electron tunneling to light capture and proton exchange as well as simpler bond breaking redox catalysis. Hope for similar solutions of more complex bioinorganic enzymes is indicated in several papers presented in this Discussion. Armed with an engineering understanding of mechanism, the current serious frustrations to successful creation of functional artificial proteins that are rooted in protein complexity can fall away. Here we discuss the genetic and biological roots of protein complexity and show how to dodge and minimize the effects of complexity. In the best-understood cases, artificial enzymes can be designed from scratch using the simplest of protein scaffolds.

Indexed as

BiocatalysisEnzymesProtein EngineeringEnzymes

Identifiers

PMID21322497
PMCPMC4073794

What OpenQuestion holds

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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.