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Chemistry

D-Index
84
Citations
20785
World Ranking
2873
National Ranking
977

Research.com Recognitions

  • 2019 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Carsten Krebs is affiliated with Pennsylvania State University in the United States. Their research spans several interconnected disciplines, primarily within biochemistry, genetics, molecular biology, materials science, and chemistry. The scientist's work focuses heavily on molecular biology, materials chemistry, and inorganic chemistry, with additional attention to fields such as renewable energy, sustainability, environment, and cell biology.

The main research topics addressed by Krebs include metal-catalyzed oxygenation mechanisms, crystallization and solubility studies, X-ray diffraction in crystallography, metalloenzymes and iron-sulfur proteins, porphyrin metabolism and disorders, microbial metabolism and enzyme function, and heme oxygenase-1 and carbon monoxide.

Krebs's publication record demonstrates involvement in a range of scientific journals and venues. Key publication outlets include:

  • The Cambridge Structural Database
  • Journal of the American Chemical Society
  • Biochemistry
  • Science
  • Nature Communications

The scientist has frequently collaborated with notable coauthors such as J. Martin Bollinger, Debangsu Sil, Amie K. Boal, C. Näther, and Molly J. McBride.

Among Krebs's recent publications are the following papers:

  • "Fe-S cofactors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets," 2021, Science
  • "A Peroxodiiron(III/III) Intermediate Mediating Both N-Hydroxylation Steps in Biosynthesis of the N-Nitrosourea Pharmacophore of Streptozotocin by the Multi-domain Metalloenzyme SznF," 2020, Journal of the American Chemical Society
  • "Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase," 2020, Nature Communications
  • "Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB," 2021, Nature
  • "Nuclear Resonance Vibrational Spectroscopic Definition of the Facial Triad FeIVO Intermediate in Taurine Dioxygenase: Evaluation of Structural Contributions to Hydrogen Atom Abstraction," 2020, Journal of the American Chemical Society

Krebs received recognition as a Fellow of the American Association for the Advancement of Science (AAAS) in 2019.

Best Publications

  • Non-heme Fe(IV)-oxo intermediates.

    Carsten Krebs;Danica Galonić Fujimori;Christopher T. Walsh;J. Martin Bollinger

  • The First Direct Characterization of a High-Valent Iron Intermediate in the Reaction of an α-Ketoglutarate-Dependent Dioxygenase: A High-Spin Fe(IV) Complex in Taurine/α-Ketoglutarate Dioxygenase (TauD) from Escherichia coli†

    John C. Price;Eric W. Barr;Bhramara Tirupati;J. Martin Bollinger

  • IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU.

    Jeffrey N. Agar;Carsten Krebs;Jeverson Frazzon;Boi Hanh Huynh

  • Evidence for Hydrogen Abstraction from C1 of Taurine by the High-Spin Fe(IV) Intermediate Detected during Oxygen Activation by Taurine:α -Ketoglutarate Dioxygenase (TauD)

    John C. Price;Eric W. Barr;Timothy E. Glass;Carsten Krebs

  • Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase

    Lee M. Hoffart;Eric W. Barr;Robert B. Guyer;J. Martin Bollinger

  • Two interconverting Fe( IV ) intermediates in aliphatic chlorination by the halogenase CytC3

    Danica P Galonić;Eric W Barr;Christopher T Walsh;J Martin Bollinger

  • EXAFS Spectroscopic Evidence for an FeO Unit in the Fe(IV) Intermediate Observed during Oxygen Activation by Taurine:α-Ketoglutarate Dioxygenase

    Pamela J. Riggs-Gelasco;John C. Price;Robert B. Guyer;Jessica H. Brehm

  • IscA, an Alternate Scaffold for Fe−S Cluster Biosynthesis†

    Carsten Krebs;Jeffrey N. Agar;Archer D. Smith;Jeverson Frazzon

  • Human calprotectin is an iron-sequestering host-defense protein

    Toshiki G Nakashige;Bo Zhang;Carsten Krebs;Elizabeth M Nolan

  • Substrate-Triggered Formation and Remarkable Stability of the C−H Bond-Cleaving Chloroferryl Intermediate in the Aliphatic Halogenase, SyrB2

    Megan L. Matthews;Courtney M. Krest;Eric W. Barr;Frédéric H. Vaillancourt

  • Spectroscopic and Computational Evaluation of the Structure of the High-Spin Fe(IV)-Oxo Intermediates in Taurine: α-Ketoglutarate Dioxygenase from Escherichia coli and Its His99Ala Ligand Variant

    Sebastian Sinnecker;Nina Svensen;Eric W. Barr;Shengfa Ye

  • Elucidation of the Fe( iv )=O intermediate in the catalytic cycle of the halogenase SyrB2

    Shaun D. Wong;Martin Srnec;Megan L. Matthews;Megan L. Matthews;Lei V. Liu

  • Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2

    Megan L. Matthews;Christopher S. Neumann;Linde A. Miles;Tyler L. Grove

  • Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen.

    Amy R. Hurshman;Carsten Krebs;Dale E. Edmondson;Boi Hanh Huynh

  • A Radically Different Mechanism for S-Adenosylmethionine–Dependent Methyltransferases

    Tyler L. Grove;Jack S. Benner;Matthew I. Radle;Jessica H. Ahlum

  • A Manganese(IV)/Iron(III) Cofactor in Chlamydia trachomatis Ribonucleotide Reductase

    Wei Jiang;Danny Yun;Lana Saleh;Eric W. Barr

  • A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay?

    Jungwon Hwang;Carsten Krebs;Boi Hanh Huynh;Dale E. Edmondson

  • Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase.

    Bekir E. Eser;Eric W. Barr;Patrick A. Frantom;Lana Saleh

  • Kinetic Dissection of the Catalytic Mechanism of Taurine:α-Ketoglutarate Dioxygenase (TauD) from Escherichia coli†

    John C. Price;Eric W. Barr;Lee M. Hoffart;Carsten Krebs

  • Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme

    Yang Zhang;Xuling Zhu;Andrew T. Torelli;Michael Lee

  • Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization

    Alice S. Pereira;William Small;Carsten Krebs;Pedro Tavares

Frequent Co-Authors

J. Martin Bollinger
J. Martin Bollinger Pennsylvania State University
Squire J. Booker
Squire J. Booker Pennsylvania State University
Edward I. Solomon
Edward I. Solomon Stanford University
Thomas Weyhermüller
Thomas Weyhermüller Max Planck Society
Christopher T. Walsh
Christopher T. Walsh Stanford University
Nicolai Lehnert
Nicolai Lehnert University of Michigan–Ann Arbor
Eckhard Bill
Eckhard Bill Max Planck Society
Amy C. Rosenzweig
Amy C. Rosenzweig Northwestern University
Dale E. Edmondson
Dale E. Edmondson Emory University
Karl Wieghardt
Karl Wieghardt Max Planck Society

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