Evidence map›Paper›PMID 21648438›Full record

ArticleThe journal of physical chemistry. A2011

Time-dependent fifth-order bands in nominally third-order 2D IR vibrational echo spectra.

Megan C Thielges, Michael D Fayer

Abstract read
In one paragraph

Article in The journal of physical chemistry. A, 2011. 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

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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.

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

Megan C ThielgesDepartment of Chemistry, Stanford University, Stanford, California 94305, USA.
Michael D Fayer

Funding

Protein, Enzyme, and Biological Water Dynamics: 2D Vibrational Echo SpectroscopyR01GM061137 · NIGMS · STANFORD UNIVERSITY · PI FAYER, MICHAEL D · 2000 to 2011
$3.1M
Protein Dynamics and Substrate Specificity in Cytochrome P450sF32GM090549 · NIGMS · STANFORD UNIVERSITY · PI THIELGES, MEGAN CORRINE · 2010 to 2012
$120k
NIGMS NIH HHS 2-R01-GM061137-09NIGMS NIH HHS F32 GM090549NIGMS NIH HHS F32-GM090549NIGMS NIH HHS R01 GM061137
6 · The paper itself

Abstract

Progress in the field of 2D IR vibrational spectroscopy has been bolstered by the production of intense mid-IR laser pulses. As higher-energy pulses are employed, a concomitant increase occurs in the likelihood of fifth-order contributions to the 2D IR spectra. We report the appearance of fifth-order signals in 2D IR spectra of CO bound to the active site of the enzyme cytochrome P450(cam) with the substrate norcamphor. Two bands with novel time dependences, one on the diagonal and one off-diagonal, are not accounted for by normal third-order interactions. These bands are associated with a ν = 1-2 vibrational transition frequency. Both bands decay to 0 and then grow back in with opposite sign. The diagonal band is positive at short time, decays to 0, reappears with negative sign, before eventually decaying to 0. The off-diagonal band is negative at short time, decays to 0, reappears positive, and then decays to 0. The appearance and time dependence of these bands are characterized. Understanding these fifth-order bands is useful because they may be misidentified with time-dependent bands that arise from other processes, such as chemical exchange, vibrational coupling, or energy transfer. The presence and unusual time dependences of the fifth-order bands are reproduced with model calculations that account for the fact that vibrational relaxation from the ν = 2 to 1 level is approximately a factor of 2 faster than that from the ν = 1 to 0 level.

Indexed as

Chemistry, PhysicalCloning, MolecularCytochrome P-450 Enzyme SystemEnergy TransferKineticsLasersModels, ChemicalNorbornanesPlasmidsPseudomonas putidaRecombinant ProteinsSpectrophotometry, InfraredSpectrum AnalysisTransformation, BacterialVibrationCytochrome P-450 Enzyme SystemNorbornanesnorcamphorRecombinant Proteins

Identifiers

PMID21648438
PMCPMC3162047

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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.