Evidence map›Paper›PMID 21568312›Full record

ArticleBiochemistry2011

Probing oxygen activation sites in two flavoprotein oxidases using chloride as an oxygen surrogate.

Phaneeswara-Rao Kommoju, Zhi-wei Chen, Robert C Bruckner, F Scott Mathews, Marilyn Schuman Jorns

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 80 citations in OpenAlex.

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  9. Tuning of pThe Journal of biological chemistry · 2020
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  10. Oxidative cyclization ofThe Journal of biological chemistry · 2018
    Article
  11. Enzymatic control of dioxygen binding and functionalization of the flavin cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase.Angewandte Chemie (International ed. in English) · 2017
    Article
  17. Article
  18. Linear and Branched PEIs (Polyethylenimines) and Their Property Space.International journal of molecular sciences · 2016
    Article
  19. Article
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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 3 institutions in 1 country.

Phaneeswara-Rao KommojuDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102, USA.
Zhi-wei Chen
Robert C Bruckner
F Scott Mathews
Marilyn Schuman Jorns
Drexel University · USSaint Louis University · USWashington University in St. Louis · US

Funding

FLAVOENZYME MECHANISMS: REDOX AND NON-REDOX REACTIONSR01GM031704 · NIGMS · MCP HAHNEMANN UNIVERSITY · PI JORNS, MARILYN S · 1985 to 2007
$2.4M
NIGMS NIH HHS GM 31704NIGMS NIH HHS R01 GM031704
6 · The paper itself

Abstract

A single basic residue above the si-face of the flavin ring is the site of oxygen activation in glucose oxidase (GOX) (His516) and monomeric sarcosine oxidase (MSOX) (Lys265). Crystal structures of both flavoenzymes exhibit a small pocket at the oxygen activation site that might provide a preorganized binding site for superoxide anion, an obligatory intermediate in the two-electron reduction of oxygen. Chloride binds at these polar oxygen activation sites, as judged by solution and structural studies. First, chloride forms spectrally detectable complexes with GOX and MSOX. The protonated form of His516 is required for tight binding of chloride to oxidized GOX and for rapid reaction of reduced GOX with oxygen. Formation of a binary MSOX·chloride complex requires Lys265 and is not observed with Lys265Met. Binding of chloride to MSOX does not affect the binding of a sarcosine analogue (MTA, methylthioactetate) above the re-face of the flavin ring. Definitive evidence is provided by crystal structures determined for a binary MSOX·chloride complex and a ternary MSOX·chloride·MTA complex. Chloride binds in the small pocket at a position otherwise occupied by a water molecule and forms hydrogen bonds to four ligands that are arranged in approximate tetrahedral geometry: Lys265:NZ, Arg49:NH1, and two water molecules, one of which is hydrogen bonded to FAD:N5. The results show that chloride (i) acts as an oxygen surrogate, (ii) is an effective probe of polar oxygen activation sites, and (iii) provides a valuable complementary tool to the xenon gas method that is used to map nonpolar oxygen-binding cavities.

Indexed as

Amino Acid SubstitutionAspergillus nigerBinding SitesCatalytic DomainChloridesCrystallography, X-RayGlucose OxidaseHydrogen BondingModels, MolecularMutagenesis, Site-DirectedOxygenRecombinant ProteinsSarcosine OxidaseSpectrophotometryChloridesGlucose OxidaseOxygenRecombinant ProteinsSarcosine Oxidase

Identifiers

PMID21568312
PMCPMC3448946
OpenAlexW1982118176

What OpenQuestion holds

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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.