Evidence map›Paper›PMID 37069165›Full record

ArticleNature communications2023

Structure and mechanism of the alkane-oxidizing enzyme AlkB.

Xue Guo, Jianxiu Zhang, Lei Han, Juliet Lee, Shoshana C Williams, Allison Forsberg, Yan Xu, Rachel Narehood Austin, Liang Feng

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
7.5field-weighted citation impact, top 1% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Pooled it
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  5. Review
  6. Paired genomic and proteomic analysis ofMicrobiology spectrum · 2026
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  20. Structural basis for anaerobic alkane activation by a multisubunit glycyl radical enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

9 authors at 4 institutions in 1 country.

Xue Guo *Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Jianxiu Zhang *Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, 94305, USA.ORCID 0000-0002-1864-7510
Lei Han *Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Juliet LeeDepartment of Chemistry, Barnard College, 3009 Broadway, New York, NY, 10027, USA.
Shoshana C WilliamsDepartment of Chemistry, Barnard College, 3009 Broadway, New York, NY, 10027, USA.ORCID 0000-0001-5669-6340
Allison ForsbergDepartment of Chemistry, Barnard College, 3009 Broadway, New York, NY, 10027, USA.
Yan XuDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Rachel Narehood AustinDepartment of Chemistry, Barnard College, 3009 Broadway, New York, NY, 10027, USA. raustin@barnard.edu.ORCID 0000-0001-9233-4443
Liang FengDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, 94305, USA. liangf@stanford.edu.ORCID 0000-0001-6171-2050
Stanford University · USBarnard College · USCalifornia Institute of Technology · USUniversity of Southern California · US

Funding

The Stanford-SLAC CryoEM Center supplementU24GM129541 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH, HEDMAN, BRITT · 2018 to 2023
$54.8M
Molecular mechanisms of alkane hydroxylase (AlkB) reactivity and selectivityR01GM130989 · NIGMS · BARNARD COLLEGE · PI AUSTIN, RACHEL NAREHOOD · 2020 to 2023
$1.2M
NIGMS NIH HHS R01 GM130989NIGMS NIH HHS U24 GM129541
6 · The paper itself

Abstract

Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms.

Indexed as

AlkanesAlkB EnzymesCarbonBiodegradation, EnvironmentalOxidation-ReductionAlkanesAlkB EnzymesCarbon

Identifiers

PMID37069165
PMCPMC10110569
OpenAlexW4366171176

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.