Evidence map›Paper›PMID 27639964›Full record

ArticleBiochimica et biophysica acta2016

Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies.

Jessica Spradlin, Diana Lee, Sruthi Mahadevan, Mavish Mahomed, Lawrence Tang, Quan Lam, Alexander Colbert, Oliver S Shafaat, David Goodin, Marco Kloos and 2 more

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

Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

8 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Coupling efficiency in light-driven hybrid P450BM3 and CYP119 enzymes.Archives of biochemistry and biophysics · 2019
    Article
  6. Keeping the spotlight on cytochrome P450.Biochimica et biophysica acta. Proteins and proteomics · 2018
    Review
  7. Article
  8. 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

12 authors at 4 institutions in 2 countries.

Jessica SpradlinSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
Diana LeeSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
Sruthi MahadevanSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
Mavish MahomedDepartment of Chemistry, One Shields Ave., University of California Davis, Davis, CA, United States.
Lawrence TangSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
Quan LamSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
Alexander ColbertSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
Oliver S ShafaatDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, United States.
David GoodinDepartment of Chemistry, One Shields Ave., University of California Davis, Davis, CA, United States.
Marco KloosDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
Mallory KatoSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
Lionel E CheruzelSan José State University, Department of Chemistry, One Washington Square, San José, CA, United States. Electronic address: lionel.cheruzel@sjsu.edu.
San Jose State University · USUniversity of California, Davis · USCalifornia Institute of Technology · USMax Planck Institute for Medical Research · DE

Funding

NOVEL SUBSTRATE OXIDATION BY ENZYME ENGINEERINGR01GM041049 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GOODIN, DAVID B. · 1994 to 2014
$3.6M
Novel Substrate Oxidation by Enzyme EngineeringR37GM041049 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GOODIN, DAVID B. · 2006 to 2010
$2.1M
Ru(II)-diimine labeled P450 mutants for the selective hydroxylation of substrateSC3GM095415 · NIGMS · SAN JOSE STATE UNIVERSITY · PI CHERUZEL, LIONEL E. · 2011 to 2018
$860k
NIGMS NIH HHS R01 GM041049NIGMS NIH HHS R37 GM041049NIGMS NIH HHS SC3 GM095415
6 · The paper itself

Abstract

backgroundIn order to perform selective CH functionalization upon visible light irradiation, Ru(II)-diimine functionalized P450 heme enzymes have been developed. The sL407C-1 enzyme containing the Ru(bpy)

methodsA combination of X-ray crystallography, site-directed mutagenesis, transient absorption measurements and enzymatic assays was used to gain insights into its photocatalytic activity and electron transfer pathway.

resultsThe crystal structure of the sL407C-1 enzyme was solved in the open and closed conformations revealing a through-space electron transfer pathway involving highly conserved, F393 and Q403, residues. Several mutations of these residues (F393A, F393W or Q403W) were introduced to probe their roles in the overall reaction. Transient absorption measurements confirm rapid electron transfer as heme reduction is observed in all four hybrid enzymes. Compared to the parent sL407C-1, photocatalytic activity was negligible in the dF393A-1 enzyme while 60% increase in activity with total turnover numbers of 420 and 90% product conversion was observed with the dQ403W-1 mutant.

conclusionsIn the sL407C-1 enzyme, the photosensitizer is ideally located to rapidly deliver electrons, using the naturally occurring electron transfer pathway, to the heme center in order to activate molecular dioxygen and sustain photocatalytic activity. GENERAL SIGNIFICANCE: The results shed light on the design of efficient light-driven biocatalysts and the approach can be generalized to other members of the P450 superfamily.

Indexed as

Amino Acid SubstitutionBacterial ProteinsCrystallography, X-RayCytochrome P-450 Enzyme SystemElectron TransportHemeKineticsModels, MolecularMutagenesis, Site-DirectedNADPH-Ferrihemoprotein ReductasePhotochemical ProcessesProtein ConformationRecombinant Fusion ProteinsSpectrophotometryBacterial ProteinsCytochrome P-450 Enzyme Systemflavocytochrome P450 BM3 monoxygenasesHemeNADPH-Ferrihemoprotein ReductaseRecombinant Fusion ProteinsCrystal structureCytochrome P450Electron transferEnzyme catalysisHybrid P450 BM3 enzymesPhotocatalytic activity

Identifiers

PMID27639964
PMCPMC5071167
OpenAlexW2519123737

What OpenQuestion holds

Textmetadata
LicenceTDM
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.