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org/JPCL Letter

Photoelectron Circular Dichroism of Electrosprayed Gramicidin

Anions
Peter Krüger, Jon Henrik Both, Uwe Linne, Fabien Chirot, and Karl-Michael Weitzel*
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ABSTRACT: Many sophisticated approaches for analyzing properties of chiral matter have
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been developed in recent years. But in general, the available chiroptical methods are limited to
either solvated or small gaseous molecules. Studying the chirality of large biopolymers in the
gas phase, including aspects of the secondary structure, becomes accessible by combining the
electrospray ionization technique with chiroptical detection protocols. Here, laser-induced
photodetachment from gramicidin anions, a peptide consisting of 15 amino acids has been
investigated. The angular distribution of photoelectrons is demonstrated to be sensitive to the
substitution of protons by cesium ions, which is accompanied by a conformational change. The
photoelectron circular dichroism (PECD) is −0.5% for bare gramicidin, whereas gramicidin
with several Cs+ ions attached exhibits a PECD of +0.5%. The results are complemented and
supported by ion mobility studies. The presented approach offers the prospect of studying
chirality and the secondary structure of various biopolymers.

N ature consists mostly of chiral molecules of a specific

absolute configuration. For example, amino acids and
sugars occur almost exclusively in their L- and D-configurations,
respectively. This homochirality has important consequences
in many scientific fields since the otherwise chemically and
physically similar enantiomers feature different properties in
chiral contexts. Mirror images of chiral pharmaceuticals often
exhibit different bioactivity in the human body.1 As a result,
enantiosensitive analytical methods are needed to study such
behavior and quantify enantiomeric purity.
These crucial tasks can be accomplished by techniques based
on the photoelectron circular dichroism (PECD). PECD
describes forward−backward asymmetries in the photoelectron
angular distribution of randomly oriented precursors along the
light propagation axis upon photoionization with circular
polarized light. The chiroptical response can be quantified by
eq 1.2
in total ion yields,27 PECD manifests in certain a laboratory
frame defined by the laser propagation axis.
Recently, PECD was measured in the photodetachment of
electrosprayed anions for the first time, using two amino acids
as examples.28 These experimental findings were subsequently
supported by theoretical model calculations.29 Within the
present study the extension of the new electrospray
ionization−PECD (ESI-PECD) technique toward the analysis
of biopolymers is demonstrated. To this end, the antibiotic
peptide gramicidin was chosen as analyte for proof of principle
experiments. Gramicidin consists of 15 amino acids and has
the following linear sequence: Formyl-L-Xaa1-D-Gly2-L-Ala3-D-
Leu4-L-Ala 5-D -Val6- L-Val7- D-Val 8-L-Trp9-D -Leu10-L-Xbb11- D-
Leu12-L-Trp13-D-Leu14-L-Trp15-ethanolamin. In the naturally
occurring substance from Bacillus brevis Xaa can be Val (80−
95%) or Ile (5−20%)30 and Xbb is Trp (80−85%), Phe (6−
7%), or Tyr (5−14%). Gramicidin is an important model

ji YLCP,F − YLCP,B YRCP,F − YRCP,B yzz

membrane protein.31
PECD = 2jjjj zz
YRCP,F + YRCP,B z{
The alteration of D- and L-amino acids in gramicidin leads to

k YLCP,F + YLCP,B
− a preferential formation of β-helices as a secondary structure.32
(1) Furthermore, gramicidin tends to form head-to-head or
double-helix dimers in the condensed phase.33 The exact
Here, YLCP/RCP,F/B denotes the electron yields in forward (F) or conformation depends inter alia on the chemical environment,
backward (B) direction with left (LCP) or right (RCP) temperature, and presence of alkali ions.33−36 The double-
circular polarization.
PECD was first predicted theoretically3 and later verified
experimentally by single4 and multiphoton ionization2,5 of Received: May 12, 2022
neutral precursors. The effect is not only sensitive to the Accepted: June 23, 2022
absolute configuration but also to conformation,6−16 chemical Published: June 27, 2022
substitution,17,18 and dimerization and clustering,19−21 as well
as vibrations.22−26 In contrast to the more conventional
circular dichroism observed either in one photon absorption or

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6110 J. Phys. Chem. Lett. 2022, 13, 6110−6116
The Journal of Physical Chemistry Letters pubs.acs.org/JPCL Letter

helical gramicidin dimers can act as a channel for monovalent the self-built linear time-of-flight mass spectrometer (TOF-
ions through cell membranes.33,37 MS). Therefore, the relative ion yield distribution was
After providing the proof of principle that the PECD of determined by means of a high-resolution mass spectrum
biopolymers can be investigated by employing electrospray that was acquired using the ion mobility spectrometer (IMS),
ionization, the conformational sensitivity of the PECD in the cf. Figure S2 and Table S3 of the Supporting Information (SI).
photodetachment of gramicidin anions will be discussed. To Neither the TOF-MS nor the IMS provided any indication of
this end, analyte solutions with different solvent compositions signals originating from gramicidin dimers under the
and salt adducts were investigated. experimental conditions. The high-resolution mass spectra do
Circular dichroism spectroscopy is a standard technique for not reveal distinct isotope patterns of dimers (Figures S2 and
determining the secondary (and tertiary) structure of S3), and only a single feature is observed in the IMS arrival
biopolymers in solution.38,39 By combining the ESI technique time distributions (Figure 7, n = 0).
with the PECD approach similar applications become possible The mass spectrum, which was obtained after interaction of
on low-density samples in the gas phase. This development will the electrosprayed ions with the laser beam, is shown as a black
facilitate investigations of solvent effects and conformational trace in Figure 1, and the resulting signal difference is depicted
dynamics. in blue. Depletion of dianions and a simultaneous signal
The ESI mass spectrum of gramicidin in a 20:80 water/ increase of monoanions are observed. These yield differences
methanol mixture without influence of the laser (red) is shown are indicative for a photodetachment of gramicidin dianions.
in Figure 1. Direction-resolved detection of the created photoelectrons
allows PECD to be quantified according to eq 1. A mean
PECD value for the precursor distribution of gramicidin
dianions electrosprayed from a 20:80 water/methanol mixture
of −0.46 ± 0.21% was determined. This small negative value
corresponds to a preferential backward emission for LCP
pulses and a preferential forward emission with RCP pulses,
respectively. The chiral response of gramicidin can be caused
by the asymmetric centers in its amino acids and possibly by a
chiral secondary structure of the peptide.
In the condensed phase gramicidin tends to form helical
dimers.33,34 Double-resonance IR-UV spectroscopy of neutral
gramicidin also suggests a family of closely related helical
conformers in the gas phase.40,41 Matheis et al. reported that
the helical structure of gramicidin is retained upon electro-
spraying, however, the helix is elongated compared to the
solution. That conclusion was based on photoelectron
spectroscopy results, employing photodetachment of electrons
as in the current work.42 In principle, each amino acid
Figure 1. ESI mass spectra (negative mode) of gramicidin in 20:80 contained in gramicidin may contribute to the PECD signal
water/methanol with laser on (black) and laser off (red) as well as the observed. Neither the amount nor the sign of this contribution
corresponding difference trace (blue). is at this point clear beyond doubt. But it seems likely that
contributions of the individual amino acids in gramicidin at
A variety of signals corresponding to the different gramicidin least partially cancel out. As a consequence it is conceivable
variants A1, A2, B1, B2, C1, and C2 are apparent in two that the PECD value measured may originate from the
separate m/z regions. For m/z ratios between 920.5 and 947 secondary structure, which in natural gramicidin is supposed to
intense signals of doubly deprotonated gramicidin ions [M − be a right-handed helix.43,44
2H]2− appear. Around a m/z ratio of ca. 1900 a number of To demonstrate the sensitivity of the PECD to the
monoanions [M − H]− are detected. The individual m/z secondary structure of biopolymer anions, different gramicidin
values of the corresponding ionic species are listed in Table 1. solutions were analyzed. First of all, the influence of differing
As expected, gramicidin A1 (Xaa = Val; Xbb = Trp) clearly solvent compositions was investigated. This approach was
dominates the mass spectrum. Not all features of less abundant chosen since the conformation and dimerization ratio of
species could be resolved due to the limited mass resolution of gramicidin in solution is strongly affected by its solvent
environment.34,35 The soft ESI technique allows one to at least
Table 1. Mass to Charge Ratios (m/z) of Singly and Doubly partially preserve such structural information.45 For example, it
Deprotonated Gramicidin Variants was shown that the homo- and heterodimer yield of gramicidin
in the gas phase depends on the solvent used for ESI in the
m/z positive mode.46,47
The electronic circular dichroism (ECD) spectra of
label [M − 2H] 2−
[M − H]− Xaa Xbb
gramicidin in pure methanol and a 50:50 water/methanol
A1 940 1881 Val Trp mixture are compared in Figure 2.
A2 947 1895 Ile Trp The ECD spectrum in pure methanol (black) is qualitatively
B1 920.5 1842 Val Phe in good agreement with literature.35,36 Distinct changes of the
B2 927.5 1856 Ile Phe spectrum are caused by the addition of water (red). The
C1 928.5 1858 Val Tyr mainly negative ellipticity below 250 nm becomes primarily
C2 935.5 1872 Ile Tyr positive. The resulting ECD spectrum in a 50:50 water/
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Figure 2. Electronic circular dichroism spectra of gramicidin in a pure
methanol solution and a 50:50 water/methanol mixture.
methanol mixture is very similar to spectra of gramicidin in
2,2,2-trifluoroethanol, where gramicidin predominantly exists
in monomeric form.32,35,46,47 This suggests that the addition of
water causes a shift of the conformational distribution of
gramicidin toward monomeric species, as observed for n-
propanol and ethanol solutions.46,47
The corresponding ESI mass spectra for the two investigated
solvent systems are very similar (Figure S1 in the SI). Only
negligible ion yield differences for weak adduct signals are
observed.
The PECD values of gramicidin dianions, which were
electrosprayed from a methanolic solution and a water/
methanol mixture, are shown in Figure 3.
Figure 3. Photoelectron circular dichroism (PECD) of gramicidin
dianions electrosprayed from pure methanol and a 50:50 water/
methanol mixture.
As for the 20:80 water/methanol mixture, small negative
PECD values were obtained in both cases. For a pure
methanolic solution a PECD of −0.46 ± 0.22% was
determined and electrospraying a 50:50 water/methanol
mixture resulted in a PECD of −0.67 ± 0.21%. Within the
error margins of the experiment, no significant influence of the
solvent composition is observed. Despite different conforma-
tional distributions in solution, similar PECD values of gaseous
gramicidin dianions are obtained after electrospray ionization.
Since PECD is generally very sensitive to conformational
changes, this observation suggests similar secondary structures
of gramicidin dianions in the gas phase. The solvent history is
presumably lost due to structural equilibration during the ion
trapping period in the current experimental setup. As a
consequence, the PECD values reported in this work can be
assumed to correspond to equilibrium gas phase conforma-
tions. In principle, information regarding the solution phase
could be accessible by reducing trapping times at the cost of
signal loss. However, this may require cooling the entire
experimental setup.48
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To manipulate the gas phase conformation of gramicidin
dianions, an excess of CsOH (2 mmol/L) was added to
corresponding analyte solutions. The resulting ESI mass
spectra for 20:80 mixtures of water and methanol are shown
in Figure 4.
Figure 4. ESI mass spectra (negative mode) of gramicidin in a 20:80
water/methanol mixture with 2 mmol/L CsOH. Spectra with laser on
and off are plotted in black and red, respectively. The corresponding
difference trace is depicted in blue.
A variety of new signals is observed. Above m/z = 940
multiple groups of signals with relative intensity distributions
as in Figure 1 are detected. The equal spacing of Δm/z = 66
between these groups is indicative for substitutions of protons
for cesium ions in gramicidin dianions. Figure 4 indicates the
replacement of up to 10 protons by Cs+ ions. This replacement
is confirmed by high-resolution ESI-MS data provided in
Figure S3 of the SI. Below m/z = 940 hydrolysis product ions
can be detected. For example, dianions with m/z = 876.5 and
m/z = 812 can result from decomposition of the peptide at the
N-terminus between Xaa-Gly and Ala-Leu, respectively.
The difference mass spectrum resulting from interaction
with UV laser pulses (Figure 4, blue) again reveals depletion of
dianionic signals caused by photodetachment. Simultaneously,
a signal increase for the monoanions within the recorded mass
region (n = 0−2) is apparent. The absolute dianion yield
differences and the percentage depletion are plotted in Figure
5 as a function of the number n of substitutions for cesium
ions. The maximum yield difference is observed for
[M − (n + 2)H + nCs]2− with n = 5. The relative signal
depletion increases approximately linearly with the number of
substitutions n, until for n ≥ 9 a virtually quantitative depletion
is observed.
Matheis et al. suggested that electrosprayed gramicidin
dianions [M − 2H]2− are deprotonated at the hydroxy group
of the C-terminus and the backbone nitrogen closest to the N-
terminus.42 Accordingly, it seems plausible that the sub-
stitution of protons for cesium ions is taking place at the
peptide backbone as well. This hypothesis is supported by the
observed amount of substitution (up to n ≈ 10) and the
continuous change of ion yields with n. In case other
deprotonation sites were involved, which are available only
in limited numbers such as tryptophan residues, a lower
maximum of n and/or a discontinuous variation of ion yields
with n would be expected.
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Figure 5. Absolute and relative depletion of baseline corrected
gramicidin dianion signals [M − (n + 2)H + nCs]2− upon laser
interaction as a function of attached cesium ions n.
The increase of the photodetachment efficiency with the
number of substitutions n is likely attributed to an increase of
the electron density in the peptide backbone by breaking
covalent N−H bonds and forming ionic N−-Cs+ pairs. Higher
electron densities could facilitate the photodetachment process
which was proposed to occur mainly from the deprotonated
backbone amide.42
For the precursor ion distribution obtained after adding 2
mmol/L CsOH to a gramicidin solution in a 20:80 mixture of
water and methanol (Figure 4) the PECD was determined.
The result (blue) is displayed in Figure 6 alongside the PECD
value of the pure gramicidin solution (red).
Figure 6. Photoelectron circular dichroism (PECD) of gramicidin
electrosprayed from a 20:80 water/methanol mixture with and
without an excess of 2 mmol/L CsOH.
In contrast to the already discussed negative PECD value of
−0.46 ± 0.21% for [M-2H]2−, a positive PECD of 0.44 ±
0.14% was determined for the distribution of [M − (n + 2)H +
nCs]2−. This change of the PECD value, i.e., the inversion of
the forward−backward asymmetry in the photoelectron
angular distribution, is caused by alterations of the molecular
potential in which the outgoing electron is scattered. In the
present case of cesium substitution, two contributions are
expected to mainly effect the PECD. On the one hand, the
change of chemical identity can play a major role. The
sensitivity of the PECD to chemical substitution was
demonstrated by comparing the PECD of trifluoromethylox-
irane and methyloxirane.18 The substitution of -CH3 and -CF3
has significant effects on the PECD. Even a sign inversion is
observed for electrons with small kinetic energies emitted from
the HOMO.18 On the other hand, due to the replacement of
small protons by larger cesium ions a conformational
adaptation of gramicidin dianions is expected. The conforma-
tional sensitivity of the PECD was studied extensively and large
effects were reported for a variety of molecules.6−13
Accordingly, changes of the secondary structure of gramicidin
dianions caused by substitution might contribute to the PECD
changes as well.
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As discussed above, gramicidin and corresponding anions
were suggested to form helical secondary structures in the gas
phase.40−42 Hence, an inversion of the sense of rotation could
explain the observed sign inversion of the PECD. Dimeric
conformers of gramicidin with opposing helicities are
commonly encountered in organic solvents.34,49 Conforma-
tional changes in solution, including helix inversion, can be
induced by binding of alkali ions such as cesium.36,49,50 The
attachment of single alkali cations to neutral gramicidin affects
the conformation and conformational preferences (e.g., β-sheet
forming tendency) as concluded from theory (molecular
dynamics simulations) and experiment (e.g., ion mobility
spectrometry).51,52
To examine the possibility of conformational alterations by
the substitution of protons for cesium ions in gramicidin
dianions, ion mobility measurements on electrosprayed
[M − (n + 2)H + nCs]2− were performed. IMS data have
been recorded with two different instruments. Data recorded
with a SYNAPT G2Si (Waters) instrument in Marburg are
presented in the main text. Data recorded with a home-built
IMS instrument in Lyon are presented in the SI. Drift time
distributions for different degrees of substitution n are
compared in Figure 7. For bare gramicidin dianions (n = 0)
Figure 7. Arrival time distribution of [M − (n + 2)H + nCs]2− signals,
with n being the number of Cs+ ions attached.
a single, slightly asymmetrical peak is observed. The fact that
the IMS data of the bare gramicidin exhibit only a single
feature indicates that the gramicidin sample is either
dominated by the A1 component or the different components
in natural gramicidin do not have markedly different properties
in the context of this work. The replacement of the first proton
for a Cs+ ion leads to a significant broadening of the arrival
time distribution (ATD) and a concomitant shift to shorter
ATD, indicating a major change to a more compact structure.
Further increasing the degree of H/Cs substitution (n = 2−6)
shifts the ATD to larger times possibly indicating a partial
unfolding of the peptide. For n = 4−6 a splitting into two not
fully separated peaks is observable. This hints at the possibility
of two different binding motives being operative. The two
components in the ATD could also reflect an equilibrium
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The Journal of Physical Chemistry Letters
between a more compact and an unfolded structural motive.
Further substitution of protons for cesium ions (n = 7 and 8)
then causes these peaks to merge again. Most likely this would
be the unfolded component.
Clear evidence for conformational changes strongly depend-
ing on the degree of substitution is provided by these IMS
results. The observed trends are supported by the second IMS
data set, which is available in Figure S4 of the SI. Those data
reveal that the collisional cross-section is about 370 Å2 for bare
gramicidin and can increase by up to 10% upon H/Cs
replacement. These findings support the hypothesis that
alterations of the secondary structure of gramicidin could be
relevant to the observed PECD change upon the addition of
CsOH.
ECD spectra of gramicidin solutions in a 20:80 water/
methanol mixture with and without 2 mmol/L CsOH are very
similar to each other (Figure S5 in the SI) and both closely
resemble the ECD spectrum for the 50:50 mixture in Figure 2.
This result supports the above conclusion that the PECD
measured with the current experimental setup is primarily
correlated to equilibrium gas phase conformations. No obvious
relation to the solution phase conformations probed by ECD
spectroscopy is found. Information about the native solution
phase conformation might be accessible by enabling softer
electrospray conditions and a faster ion transfer. We further
note that the chirality properties of electrosprayed anions of
DNA oligonucleotides can also be detected as the CD in total
electron yields recorded in photodetachment.53
PECD measurements of a biopolymer were reported by
utilization of an ESI source. Dianions of gramicidin [M −
2H]2− exhibit a small negative PECD of −0.5 ± 0.2%. The
presented extension of the analytical scope is of particular
interest because the PECD effect is highly sensitive to
conformation, as was shown for a variety of neutral precursor
molecules.6−13 Consequently, the ESI-PECD approach is a
new tool available for studying the complex conformational
behavior of relevant biological samples. The secondary (and
tertiary) structure of biopolymers is generally related to their
functionality and therefore of great interest. For example, in
the case of gramicidin its helical conformations enable the ion
channel functionality.33
In the current experimental setup, the observable PECD
value is sensitive to equilibrium gas phase conformations, as
the solvent history is presumably lost during long ion trapping
periods. This conclusion is based on contrary results for the
ECD in solution and the PECD in the gas phase. For
gramicidin in pure methanol and in a water/methanol mixture
different ECD spectra were obtained, while electrospraying
such solutions resulted in indistinguishable PECD values.
By substitution of protons for cesium ions in gramicidin
dianions, a change of the PECD can be induced. The observed
inversion of the forward−backward asymmetry in the photo-
electron angular distribution can be caused by changes of the
conformation and/or chemical identity.
Experimental evidence for conformational alterations of
gramicidin dianions upon the substitution of H+ for Cs+ is
provided by ion mobility spectrometry. Here, IMS measure-
ments of gramicidin and corresponding Cs adducts gave strong
evidence that the gas phase structure of the peptide changes
upon Cs binding, which could explain the observed behavior.
Additional investigations of the conformational sensitivity of
the ESI-PECD technique will be performed by implementing a
precursor ion mass selection to measure the PECD as a
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pubs.acs.org/JPCL Letter
function of the number of cesium substitutions n. In the
current setup this is not feasible since the ion trap does not
provide the option of mass selection. Furthermore, inducing
helix breaker amino acids, e.g., proline, into the gramicidin
sequence could give insight into the contributions from the
primary and secondary structures of gramicidin to the
observable PECD. Future work along the method demon-
strated in this work may shed new light on the dynamics of
structural changes including folding and unfolding of proteins,
e.g., by manipulating the time ions spent in the environment of
the ESI beam.
■
EXPERIMENTAL METHODS
The experimental setup was described in detail recently.28
Briefly, anions were generated by electrospray ionization of 50
μmol/L gramicidin in water/methanol mixtures (0:100, 20:80,
and 50:50). With the exception of 20:80 mixtures, NaOH (50
μmol/L) was used as an additive. In the case of 20:80 mixtures,
either no salt or an excess of 2 mmol/L CsOH was dissolved.
Electrosprayed ions are accumulated in a linear octopole trap
for 50 ms. After extraction by a field pulse, ion packages can
interact with elliptically polarized nanosecond laser pulses
inside a chirality spectrometer. A frequency tripled Nd:YAG
laser with a wavelength of 355 nm and a repetition rate of 10
Hz was used as light source. For acquiring difference mass
spectra, pulse energies of 42 mJ were used. PECD measure-
ments were performed using pulse energies of 18 mJ. Left and
right elliptically polarized laser pulses were generated by means
of a quarter wave plate. Created photoelectrons can be
detected by a microchannel plate detector. Resolving the
electron yields emitted in forward and backward directions
relative to the laser propagation direction on two separate half-
circle anodes allows the determination of PECD. The electron
image is centered on the detector by a set of deflection plates.
Remaining imperfections are canceled out by symmetrization
according to eq 1. A single measurement, called a pass, consists
of 300 laser shots with each laser helicity. Mean PECD values
and standard errors were obtained by averaging multiple passes
(see Table S1 in the SI). Changes of ion yields can be
monitored by means of a three-stage linear time-of-flight mass
spectrometer. Acquired mass spectra were smoothed by using a
quadratic Savitzky−Golay filter54 with a window length of 11.
Gramicidin from Bacillus aneurinolyticus (Bacillus brevis) was
purchased from Sigma-Aldrich as a mixture of the naturally
occurring peptide variants and used without further
purification.
ECD spectra of gramicidin solutions were acquired using a
commercial Jasco J-815 spectrometer.
Ion mobility mass spectra of gramicidin and corresponding
Cs adducts were acquired using a Synapt G2Si mass
spectrometer (Waters, U.K.). Samples were infused using the
built-in syringe pump at a flow rate of 10 μL/min. Ions were
measured in negative ion mode. Detailed measuring parame-
ters used are summarized in Table S2 of the Supporting
Information. The sample cone voltage turned out to be critical
for obtaining high-resolution spectra.
■
ASSOCIATED CONTENT
* Supporting Information
sı
The Supporting Information is available free of charge at
https://pubs.acs.org/doi/10.1021/acs.jpclett.2c01437.
https://doi.org/10.1021/acs.jpclett.2c01437
J. Phys. Chem. Lett. 2022, 13, 6110−6116
The Journal of Physical Chemistry Letters
Experimental details, ESI mass spectra of gramicidin in
different solvents, high resolution mass spectra, ion
mobility data, ECD spectra of gramicidin with and
without CsOH, and photoion circular dichroism (PDF)
Transparent Peer Review report available (PDF)
■
AUTHOR INFORMATION
Corresponding Author
Karl-Michael Weitzel − Department of Chemistry, Philipps-
Universität Marburg, 35043 Marburg, Germany;
orcid.org/0000-0002-1560-235X; Email: weitzel@
chemie.uni-marburg.de
Authors
Peter Krüger − Department of Chemistry, Philipps-Universität
Marburg, 35043 Marburg, Germany; Present
Address: Spectroscopy of Cold Molecules Department,
Institute for Molecules and Materials, Radboud University
Nijmegen, NL-6500 GL Nijmegen, The Netherlands;
orcid.org/0000-0002-6735-8790
Jon Henrik Both − Department of Chemistry, Philipps-
Universität Marburg, 35043 Marburg, Germany
Uwe Linne − Department of Chemistry, Philipps-Universität
Marburg, 35043 Marburg, Germany
Fabien Chirot − Institut Lumière Matière, UMR5306
Université de Lyon, Université Lyon 1, CNRS, 69100
Villeurbanne, France; orcid.org/0000-0001-9115-9233
Complete contact information is available at:
https://pubs.acs.org/10.1021/acs.jpclett.2c01437
Funding
A Kekulé scholarship was awarded to P.K. by Fonds der
Chemischen Industrie (FCI).
Notes
The authors declare no competing financial interest.
■
ACKNOWLEDGMENTS
We gratefully acknowledge Prof. Stephan Schiller (Heinrich-
Heine-Universität Düsseldorf) for providing the ESI source
and Dr. Sven-A. Freibert (Philipps-Universität Marburg) for
assistance with the ECD measurements at the core facility for
protein spectroscopy in the institute of cytobiology. Fruitful
discussion with Prof. Ulrich Koert (Philipps-Universität
Marburg) is gratefully acknowledged.
■
ABBREVIATIONS
ECD, electronic circular dichroism; ESI, electrospray ioniza-
tion; IMS, ion mobility spectrometry; LCP, left circular
polarization; PECD, photoelectron circular dichroism; RCP,
right circular polarization; TOF-MS, time-of-flight mass
spectrometer
■
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