Watching Alkaline Phosphatase Catalysis Through Its Vibrational Fingerprint.

Margherita Tamagnini, Haoyue Jiang, Liana Klivansky, Carlos Bustamante, Alessandra Lanzara

Abstract read

In one paragraph

Article in Biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Bioinspired silk-catechol-enzyme co-assemblies as jigsaw-designed conformation-locking bioactive-biocatalytic platforms.Bioactive materials · 2026
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

5 authors.

Margherita TamagniniDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Haoyue JiangApplied Science Technology, University of California, Berkeley, CA 94720, USA.ORCID 0000-0001-9104-7354

Liana KlivanskyMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.ORCID 0009-0005-2514-2878

Carlos BustamanteDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Alessandra LanzaraMaterials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.ORCID 0000-0002-9519-8974

Funding

Gordon and Betty Moore Foundation EPiQS Initiative GBMF4859

6 · The paper itself

Abstract

Despite decades of structural and kinetic characterization, the full spectral molecular vibrations that accompany the catalysis in alkaline phosphatase (ALP) have remained largely unexplored. In this study, we combine in situ real-time attenuated total reflection Fourier transform infrared (ATR-FTIR) measurements over a large energy range to track the hydrolysis of p-nitrophenyl phosphate (PNPP) and inorganic phosphate (Pi) over a large range of enzyme concentrations. From the static spectra of the pure components (ALP, PNPP, PNP, Pi), we identify their characteristic vibrational frequencies and use them as reference points for the time-resolved spectra. The reaction reveals a monotonic growth of the inorganic-phosphate band at 1077 cm

Indexed as

alkaline phosphatase (ALP)Fourier transform infrared spectroscopy (FTIR)molecular fingerprintingp-nitrophenyl phosphate (PNPP)spectral analysis

Identifiers

PMID41514909

DOI10.3390/biology15010068

PMCPMC12785024

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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.