Jeffrey M. Peloquin

2.0k total citations
27 papers, 1.6k citations indexed

About

Jeffrey M. Peloquin is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Cellular and Molecular Neuroscience. According to data from OpenAlex, Jeffrey M. Peloquin has authored 27 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 13 papers in Atomic and Molecular Physics, and Optics and 6 papers in Cellular and Molecular Neuroscience. Recurrent topics in Jeffrey M. Peloquin's work include Photosynthetic Processes and Mechanisms (23 papers), Spectroscopy and Quantum Chemical Studies (13 papers) and Photoreceptor and optogenetics research (6 papers). Jeffrey M. Peloquin is often cited by papers focused on Photosynthetic Processes and Mechanisms (23 papers), Spectroscopy and Quantum Chemical Studies (13 papers) and Photoreceptor and optogenetics research (6 papers). Jeffrey M. Peloquin collaborates with scholars based in United States and France. Jeffrey M. Peloquin's co-authors include R. David Britt, Kristy A. Campbell, Aileen K. W. Taguchi, Neal W. Woodbury, Vincent L. Pecoraro, William H. Armstrong, David Randall, R. G. Alden, James P. Allen and Xiaomei Lin and has published in prestigious journals such as Journal of the American Chemical Society, Biochemistry and The Journal of Physical Chemistry.

In The Last Decade

Jeffrey M. Peloquin

26 papers receiving 1.6k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Jeffrey M. Peloquin United States	19	1.3k	771	493	420	276	27	1.6k
Curtis W. Hoganson United States	21	1.4k 1.1×	564 0.7×	717 1.5×	443 1.1×	316 1.1×	28	2.0k
Warren F. Beck United States	25	1.3k 1.0×	945 1.2×	210 0.4×	524 1.2×	214 0.8×	70	1.8k
Asako Kawamori Japan	23	998 0.7×	715 0.9×	294 0.6×	387 0.9×	99 0.4×	105	1.6k
Klaus‐Dieter Irrgang Germany	20	1.3k 1.0×	677 0.9×	285 0.6×	446 1.1×	268 1.0×	30	1.6k
Hiroyuki Mino Japan	21	975 0.7×	492 0.6×	223 0.5×	362 0.9×	184 0.7×	80	1.2k
Jean‐Luc Zimmermann France	18	947 0.7×	500 0.6×	309 0.6×	377 0.9×	145 0.5×	29	1.2k
Roehl M. Cinco United States	13	998 0.7×	512 0.7×	592 1.2×	215 0.5×	364 1.3×	20	1.4k
Hiroshi Isobe Japan	28	1.5k 1.1×	1.1k 1.5×	867 1.8×	389 0.9×	436 1.6×	98	2.3k
William Ames Germany	13	936 0.7×	599 0.8×	417 0.8×	292 0.7×	321 1.2×	17	1.3k
A. M. Hawthornthwaite-Lawless United Kingdom	5	1.9k 1.4×	930 1.2×	155 0.3×	711 1.7×	358 1.3×	6	2.6k

Countries citing papers authored by Jeffrey M. Peloquin

Since Specialization

Citations

This map shows the geographic impact of Jeffrey M. Peloquin's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Jeffrey M. Peloquin with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Jeffrey M. Peloquin more than expected).

Fields of papers citing papers by Jeffrey M. Peloquin

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jeffrey M. Peloquin. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Jeffrey M. Peloquin. The network helps show where Jeffrey M. Peloquin may publish in the future.

Co-authorship network of co-authors of Jeffrey M. Peloquin

This figure shows the co-authorship network connecting the top 25 collaborators of Jeffrey M. Peloquin. A scholar is included among the top collaborators of Jeffrey M. Peloquin based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Jeffrey M. Peloquin. Jeffrey M. Peloquin is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Rappaport, Fabrice, Alain Boussac, Dee Ann Force, et al.. (2009). Probing the Coupling between Proton and Electron Transfer in Photosystem II Core Complexes Containing a 3-Fluorotyrosine. Journal of the American Chemical Society. 131(12). 4425–4433. 61 indexed citations

Slupe, Andrew M., Berea A. R. Williams, Laura M. Lee, et al.. (2005). Reduction of 13-Deoxydoxorubicin and Daunorubicinol Anthraquinones by Human Carbonyl Reductase. Cardiovascular Toxicology. 5(4). 365–376. 20 indexed citations

Britt, R. David, Kristy A. Campbell, Jeffrey M. Peloquin, et al.. (2004). Recent pulsed EPR studies of the Photosystem II oxygen-evolving complex: implications as to water oxidation mechanisms. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1655(1-3). 158–171. 182 indexed citations

Peloquin, Jeffrey M. & R. David Britt. (2001). EPR/ENDOR characterization of the physical and electronic structure of the OEC Mn cluster. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1503(1-2). 96–111. 165 indexed citations

Hung, Shao‐Ching, et al.. (2000). ESEEM studies of succinate:ubiquinone reductase from Paracoccus denitrificans. JBIC Journal of Biological Inorganic Chemistry. 5(5). 593–602. 8 indexed citations

Britt, R. David, Jeffrey M. Peloquin, & Kristy A. Campbell. (2000). Pulsed and Parallel-Polarization EPR Characterization of the Photosystem II Oxygen-Evolving Complex. Annual Review of Biophysics and Biomolecular Structure. 29(1). 463–495. 98 indexed citations

Debus, Richard J., et al.. (1999). Histidine 332 of the D1 Polypeptide Modulates the Magnetic and Redox Properties of the Manganese Cluster and Tyrosine Y_Z in Photosystem II. Biochemistry. 39(2). 470–478. 31 indexed citations

Peloquin, Jeffrey M., Xiao-Song Tang, Bruce A. Diner, & R. David Britt. (1999). An Electron Spin−Echo Envelope Modulation (ESEEM) Study of the Q_A Binding Pocket of PS II Reaction Centers from Spinach and Synechocystis. Biochemistry. 38(7). 2057–2067. 15 indexed citations

Campbell, Kristy A., et al.. (1998). The 23 and 17 kDa Extrinsic Proteins of Photosystem II Modulate the Magnetic Properties of the S₁-State Manganese Cluster. Biochemistry. 37(15). 5039–5045. 54 indexed citations

10.

Campbell, Kristy A., et al.. (1998). Parallel Polarization EPR Detection of an S₁-State “Multiline” EPR Signal in Photosystem II Particles from Synechocystis sp. PCC 6803. Journal of the American Chemical Society. 120(2). 447–448. 65 indexed citations

11.

Peloquin, Jeffrey M., Kristy A. Campbell, & R. David Britt. (1998). ⁵⁵Mn Pulsed ENDOR Demonstrates That the Photosystem II “Split” EPR Signal Arises from a Magnetically-Coupled Mangano−Tyrosyl Complex. Journal of the American Chemical Society. 120(27). 6840–6841. 89 indexed citations

12.

Campbell, Kristy A., Jeffrey M. Peloquin, Bruce A. Diner, et al.. (1997). The τ-Nitrogen of D2 Histidine 189 is the Hydrogen Bond Donor to the Tyrosine Radical Y_D^• of Photosystem II. Journal of the American Chemical Society. 119(20). 4787–4788. 65 indexed citations

13.

Peloquin, Jeffrey M., JoAnn C. Williams, Xiaomei Lin, et al.. (1994). Time-dependent thermodynamics during early electron transfer in reaction centers from Rhodobacter sphaeroides.. Biochemistry. 33(26). 8089–8100. 110 indexed citations

14.

Woodbury, Neal W., Jeffrey M. Peloquin, R. G. Alden, et al.. (1994). Relationship between thermodynamics and mechanism during photoinduced charge separation in reaction centers from Rhodobacter sphaeroides.. Biochemistry. 33(26). 8101–8112. 82 indexed citations

15.

Taguchi, Aileen K. W., Jonathan W. Stocker, R. G. Alden, et al.. (1992). Biochemical characterization and electron-transfer reactions of sym1, a Rhodobacter capsulatus reaction center symmetry mutant which affects the initial electron donor. Biochemistry. 31(42). 10345–10355. 62 indexed citations

16.

Peloquin, Jeffrey M., Edward J. Bylina, Douglas C. Youvan, & David F. Bocian. (1991). Effects of pigment-protein interactions on the conformation of the primary electron acceptor in Rhodobacter capsulatus reaction centers. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1056(1). 85–88. 5 indexed citations

17.

Peloquin, Jeffrey M., et al.. (1990). Temperature-dependent conformational changes in the bacteriopheophytins of Rhodobacter sphaeroides reaction centers. Biochemistry. 29(20). 4892–4898. 11 indexed citations

18.

Peloquin, Jeffrey M., Edward J. Bylina, Douglas C. Youvan, & David F. Bocian. (1990). Resonance Raman studies of genetically modified reaction centers from Rhodobacter capsulatus. Biochemistry. 29(36). 8417–8424. 7 indexed citations

19.

Bocian, David F., et al.. (1989). Resonance Raman Studies Of Copper(II) Octaethylisobacteriochlorin. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 1057. 146–146.

20.

Shen, Quang, Jeffrey M. Peloquin, Svein Samdal, et al.. (1988). The Molecular Structures and Conformations of Chlorocyclohexane and Bromocyclohexane as Determined by Gas-Phase Electron Diffraction.. Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry. 42a. 367–373. 24 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

Explore authors with similar magnitude of impact