About

Michael P. Hendrich is a Professor of Chemistry at Carnegie Mellon University within the Mellon College of Science. He earned his Ph.D. from the University of Illinois in 1988. His research focuses on spectroscopic and biophysical chemistry, enzymatic mechanisms, bioinorganic chemistry, and metalloenzymes. Hendrich's work aims to achieve an atomic level understanding of catalytic function in metalloproteins, which are essential for processes such as DNA synthesis, metabolism, photosynthesis, detoxification, and the chemical transformations of nitrogen, oxygen, and carbon molecules. His approach involves isolating and spectroscopically characterizing reaction intermediates of enzymes and biomimetic complexes, utilizing techniques such as EPR, ENDOR, Mössbauer spectroscopy, and SQUID magnetization. He has developed new spectroscopic instrumentation, computer simulation software, and methodologies tailored to probe metalloproteins and metal complexes. Hendrich has been a faculty member at Carnegie Mellon University since 1994, serving as an Assistant Professor, Associate Professor, and currently as a Professor since 2008. His contributions include advancing the understanding of metalloproteins' catalytic functions, which are vital for health, agriculture, and environmental processes. His research has significant implications for understanding metal imbalances and enzyme activity related to various diseases, emphasizing the importance of metalloproteins in biological and environmental contexts.

Research topics

• Chemistry
• Organic chemistry
• Stereochemistry
• Computational chemistry
• Biochemistry
• Crystallography
• Nanotechnology
• Thermodynamics
• Metallurgy
• Condensed matter physics
• Physics
• Nuclear magnetic resonance
• Inorganic chemistry
• Materials science

Selected publications

• CCDC 2457357: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-01-15

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• CCDC 2457362: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-01-15

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• CCDC 2457360: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-01-15

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• CCDC 2457361: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-01-15

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• CCDC 2457359: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-01-15

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• Author response for "Reactivity of canonical bacterial cytochrome c peroxidases: insights into the electronic structure of Compound I"

  2025-02-05

  peer-review
  PublisherDOI

• Reactivity of canonical bacterial cytochrome <i>c</i> peroxidases: insights into the electronic structure of compound I

  Chemical Science · 2025-01-01 · 5 citations

  articleOpen access

  Bacterial cytochrome c peroxidase (bCcP) family members include di-heme enzymes that are capable of producing various high oxidation states in their reactions with the substrate H 2 O 2 .

  PublisherDOI

• Steric and Electronic Modulation of Iron Complexes via Chalcogen Atom Substitution in the Secondary Coordination Sphere

  Zeitschrift für anorganische und allgemeine Chemie · 2025-12-09

  article

  The secondary coordination sphere surrounding metal centers has been shown to have a regulatory effect on the structure and function of metal complexes. In this study, we report the preparation of Fe complexes supported by a new tripodal ligand N , N ′, N ″‐[nitrilotris(ethane‐2,1‐diyl)]tris( P , P ‐diphenylthiophosphinic amido) ([psat] 3– ) that features thiophosphinic (PS) amido groups. This ligand was designed to evaluate the effect of chalcogen substitution on the coordination chemistry of iron complexes when compared to analogous species that have been previously reported with the phosphinic (PO) amido ligand system, N , N ′, N ″‐[nitrilotris(ethane‐2,1‐diyl)]tris( P , P ‐diphenylphosphinic amido) ([poat] 3– ). Although this variation had minimal impact on the structural and electronic properties of Fe(II) centers, their oxidative chemistry was found to be different, which isattributed to change in the chalcogen atoms within the secondary coordination sphere.

  PublisherDOI

• Author response for "Detection and characterization of a compound 1 species from the &lt;i&gt;c&lt;/i&gt;-type heme enzyme cytochrome &lt;i&gt;c&lt;/i&gt;′&lt;sub&gt;β&lt;/sub&gt;"

  2025-06-24

  peer-reviewSenior author
  PublisherDOI

• Detection and characterization of a compound 1 species from the <i>c</i> -type heme enzyme cytochrome <i>c</i> ′ _β

  Chemical Science · 2025-01-01 · 1 citations

  articleOpen accessSenior authorCorresponding

  Cytochrome c ′ β of the ammonia-oxidizing bacterium Nitrosomonas europaea is an enzyme containing heme c and a member of the P460 superfamily. During reaction with H 2 O 2 a key intermediate, compound 1, was trapped and spectroscopically characterized.

  PublisherOA PDFDOI

Recent grants

• NIH Grant R01GM049970

  NIH · $547k · 2003

• NIH Grant F32GM012996

  NIH · $49k

• EPR and Mössbauer Characterization of Mn and Fe Enzymes, Biomimetic Models, and Intermediates

  NIH · $2.9M · 2006–2021

• MRI: Acquisition of an Electron Paramagnetic Resonance (EPR) Spectrometer

  NSF · $305k · 2011–2014

• NIH Grant R29GM049970

  NIH · $497k · 1999

Frequent coauthors

• A. S. Borovik

  128 shared

• Joseph W. Ziller

  University of California, Irvine

  53 shared

• Andrew C. Weitz

  49 shared

• Dongwhan Lee

  Seoul National University

  48 shared

• Stephen J. Lippard

  43 shared

• Lawrence Que

  42 shared

• Eckard Münck

  Carnegie Mellon University

  42 shared

• Brad S. Pierce

  University of Alabama

  36 shared

Education

• Ph.D.

  University of Illinois

  1988

Awards & honors

• Searle Scholar Award (1995)