World's Best Scientists 2026 revealed!

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Chemistry

D-Index
53
Citations
7341
World Ranking
13328
National Ranking
3490

Overview

Joann Sanders-Loehr is affiliated with Portland State University in the United States. Their research profile does not include specific recent papers, co-authors, or publication venues in the available data.

There are no recorded book publications or awards listed in the current data. Similarly, no detailed information about main fields of study, subfields, or main topics of work has been provided.

Based on the source data, the overview focuses on the affiliation and the absence of bibliometric details such as publication counts or areas of specialization.

Best Publications

  • The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy

    Gabriele Backes;Yoshiki Mino;Thomas M. Loehr;Terrence E. Meyer

  • Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins.

    Brian G. Fox;John Shanklin;Jingyuan Ai;Thomas M. Loehr

  • Electronic and Raman spectroscopic properties of oxo-bridged dinuclear iron centers in proteins and model compounds

    Joann Sanders-Loehr;William D. Wheeler;Andrew K. Shiemke;Bruce A. Averill

  • Peroxodiferric intermediate of stearoyl-acyl carrier protein delta 9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation.

    J. A. Broadwater;Jingyuan Ai;T. M. Loehr;J. Sanders-Loehr

  • Glyoxal Oxidase From Phanerochaete Chrysosporium Is a New Radical-Copper Oxidase

    Mei M. Whittaker;Philip J. Kersten;Nobuhumi Nakamura;Joann Sanders-Loehr

  • Spectroscopic and magnetic studies of the purple acid phosphatase from bovine spleen

    Bruce A. Averill;James C. Davis;Sudhir Burman;Teresa Zirino

  • (μ-Oxo)(μ-carboxylato)diiron(III) Complexes with Distinct Iron Sites. Consequences of the Inequivalence and Its Relevance to Dinuclear Iron-Oxo Proteins

    Richard E. Norman;Shiping Yan;Lawrence Que;Gabriele Backes

  • The Catalytic Center in Nitrous Oxide Reductase, CuZ, Is a Copper−Sulfide Cluster†

    Tim Rasmussen;Ben C. Berks;Joann Sanders-Loehr;David M. Dooley

  • Raman Spectroscopy as an Indicator of Cu-S Bond Length in Type 1 and Type 2 Copper Cysteinate Proteins

    Colin R. Andrew;Hyeyeong Yeom;Joan Selverstone Valentine;B. Goeran Karlsson

  • Active site structures of deoxyhemerythrin and oxyhemerythrin

    Ronald E. Stenkamp;Larry C. Sieker;L. H. Jensen;John D. McCallum

  • Raman spectral evidence for a mu-oxo bridge in the binuclear iron center of ribonucleotide reductase.

    B M Sjöberg;T M Loehr;J Sanders-Loehr

  • Resonance Raman study of oxyhemerythrin and hydroxomethemerythrin. Evidence for hydrogen bonding of ligands to the iron-oxygen-iron center.

    Andrew K. Shiemke;Thomas M. Loehr;Joann. Sanders-Loehr

  • Resonance Raman excitation profiles indicate multiple Cys → Cu charge transfer transitions in type 1 copper proteins

    Jane Han;Thomas M. Loehr;Yi Lu;Joan Selverstone Valentine

  • A hemerythrin-like domain in a bacterial chemotaxis protein.

    Junjie Xiong;Donald M. Kurtz;Jingyuan Ai;Joann Sanders-Loehr

  • Common Oxygen Binding Site in Hemocyanins from Arthropods and Mollusks. Evidence from Raman Spectroscopy and Normal Coordinate Analysis

    Jinshu Ling;Lisa P. Nestor;Roman S. Czernuszewicz;Thomas G. Spiro

  • Structure of the binuclear iron complex in metazidohaemerythrin from Themiste dyscritum at 2.2. Å resolution

    R. E. Stenkamp;L. C. Siecker;L. H. Jensen;J. Sanders-Loehr

  • Resonance Raman study of the .mu.-oxo-bridged binuclear iron center in oxyhemerythrin

    Andrew K. Shiemke;Thomas M. Loehr;Joann Sanders-Loehr

  • Resonance Raman spectra of plastocyanin and pseudoazurin: evidence for conserved cysteine ligand conformations in cupredoxins (blue copper proteins).

    Jane Han;Elinor T. Adman;Teruhiko Beppu;Rachel Codd

  • Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant.

    Hongbin Liu;Haining Zhu;Daryl K. Eggers;Aram M. Nersissian

  • Dioxygen is the source of the mu-oxo bridge in iron ribonucleotide reductase.

    M Sahlin;B M Sjöberg;T M Loehr

Frequent Co-Authors

Gerard W. Canters
Gerard W. Canters Leiden University
Judith P. Klinman
Judith P. Klinman University of California, Berkeley
Johannis A. Duine
Johannis A. Duine Delft University of Technology
Ronald E. Stenkamp
Ronald E. Stenkamp University of Washington
Pierre Moënne-Loccoz
Pierre Moënne-Loccoz Oregon Health & Science University
Victor L. Davidson
Victor L. Davidson University of Central Florida
Donald M. Kurtz
Donald M. Kurtz The University of Texas at San Antonio
Britt-Marie Sjöberg
Britt-Marie Sjöberg Stockholm University
Brian G. Fox
Brian G. Fox University of Wisconsin–Madison
Edward A. Stern
Edward A. Stern University of Washington

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