NMR of paramagnetic metalloproteins in solution: Ubi venire, quo vadis?

Metalloproteins represent a substantial fraction of the proteome where they have an outsized contribution to enzymology. This stems from the reactivity of transition metals found in the active sites of numerous classes of enzymes that undergo redox and/or spin-state transitions. Notwithstanding, NMR...

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Published inJournal of inorganic biochemistry Vol. 234; p. 111871
Main Authors Trindade, Inês B., Coelho, Anaísa, Cantini, Francesca, Piccioli, Mario, Louro, Ricardo O.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.09.2022
Subjects
Electronic structure
Metal homeostasis and trafficking
Metalloproteins
NMR spectroscopy
Paramagnetic
Structural biology
Electronic structure
Metal homeostasis and trafficking
NMR spectroscopy
Metalloproteins
Structural biology
Paramagnetic
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Abstract Metalloproteins represent a substantial fraction of the proteome where they have an outsized contribution to enzymology. This stems from the reactivity of transition metals found in the active sites of numerous classes of enzymes that undergo redox and/or spin-state transitions. Notwithstanding, NMR structures of metalloproteins deposited in the PDB are under-represented and NMR studies exploring paramagnetic states are a minute fraction of the overall database content. This state of affairs contrasts with the early recognition that paramagnetic proteins offer unique opportunities for structure-function studies which are not available for diamagnetic proteins. Recent development of novel pulse sequences that minimize quenching of signal intensity that arises from the presence of a paramagnetic center in metalloproteins is extending even further the range of systems which can be studied by solution-state NMR. In this manuscript we review solution-state NMR applications to paramagnetic proteins, highlighting the developments in both methodologies and data interpretation, laying bare the vast range of opportunities for paramagnetic NMR to contribute to the understanding of structure and function of metalloenzymes and biomimetic metallocatalysts. Like Janus, the Roman god of transition between old and new, biomolecular paramagnetic NMR spectroscopy is transitioning from the old vision of impossibly broad lines and dramatic chemical shifts to a vision of unique opportunities to explore the structure, function, dynamics and assembly of metalloproteins in vitro and in vivo. [Display omitted] •NMR structures of paramagnetic metalloproteins are under-represented in the pdb.•New experimental methods enhance the capacity to investigate paramagnetic systems.•Theoretical framework allows the interpretation of the paramagnetic effects.•Paramagnetic effects offer unique opportunities for structure-function studies.•Numerous key enzymes are metalloproteins and the field is ripe for exploration.
AbstractList Metalloproteins represent a substantial fraction of the proteome where they have an outsized contribution to enzymology. This stems from the reactivity of transition metals found in the active sites of numerous classes of enzymes that undergo redox and/or spin-state transitions. Notwithstanding, NMR structures of metalloproteins deposited in the PDB are under-represented and NMR studies exploring paramagnetic states are a minute fraction of the overall database content. This state of affairs contrasts with the early recognition that paramagnetic proteins offer unique opportunities for structure-function studies which are not available for diamagnetic proteins. Recent development of novel pulse sequences that minimize quenching of signal intensity that arises from the presence of a paramagnetic center in metalloproteins is extending even further the range of systems which can be studied by solution-state NMR. In this manuscript we review solution-state NMR applications to paramagnetic proteins, highlighting the developments in both methodologies and data interpretation, laying bare the vast range of opportunities for paramagnetic NMR to contribute to the understanding of structure and function of metalloenzymes and biomimetic metallocatalysts.
Metalloproteins represent a substantial fraction of the proteome where they have an outsized contribution to enzymology. This stems from the reactivity of transition metals found in the active sites of numerous classes of enzymes that undergo redox and/or spin-state transitions. Notwithstanding, NMR structures of metalloproteins deposited in the PDB are under-represented and NMR studies exploring paramagnetic states are a minute fraction of the overall database content. This state of affairs contrasts with the early recognition that paramagnetic proteins offer unique opportunities for structure-function studies which are not available for diamagnetic proteins. Recent development of novel pulse sequences that minimize quenching of signal intensity that arises from the presence of a paramagnetic center in metalloproteins is extending even further the range of systems which can be studied by solution-state NMR. In this manuscript we review solution-state NMR applications to paramagnetic proteins, highlighting the developments in both methodologies and data interpretation, laying bare the vast range of opportunities for paramagnetic NMR to contribute to the understanding of structure and function of metalloenzymes and biomimetic metallocatalysts. Like Janus, the Roman god of transition between old and new, biomolecular paramagnetic NMR spectroscopy is transitioning from the old vision of impossibly broad lines and dramatic chemical shifts to a vision of unique opportunities to explore the structure, function, dynamics and assembly of metalloproteins in vitro and in vivo. [Display omitted] •NMR structures of paramagnetic metalloproteins are under-represented in the pdb.•New experimental methods enhance the capacity to investigate paramagnetic systems.•Theoretical framework allows the interpretation of the paramagnetic effects.•Paramagnetic effects offer unique opportunities for structure-function studies.•Numerous key enzymes are metalloproteins and the field is ripe for exploration.
ArticleNumber 111871
Author Cantini, Francesca
Piccioli, Mario
Trindade, Inês B.
Coelho, Anaísa
Louro, Ricardo O.
Author_xml – sequence: 1
  givenname: Inês B.
  surname: Trindade
  fullname: Trindade, Inês B.
  organization: Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157 Oeiras, Portugal
– sequence: 2
  givenname: Anaísa
  surname: Coelho
  fullname: Coelho, Anaísa
  organization: Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157 Oeiras, Portugal
– sequence: 3
  givenname: Francesca
  surname: Cantini
  fullname: Cantini, Francesca
  organization: Department of Chemistry, Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
– sequence: 4
  givenname: Mario
  surname: Piccioli
  fullname: Piccioli, Mario
  email: piccioli@cerm.unifi.it
  organization: Department of Chemistry, Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
– sequence: 5
  givenname: Ricardo O.
  surname: Louro
  fullname: Louro, Ricardo O.
  email: louro@itqb.unl.pt
  organization: Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157 Oeiras, Portugal
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Keywords Electronic structure
Metal homeostasis and trafficking
NMR spectroscopy
Metalloproteins
Structural biology
Paramagnetic
Language English
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Copyright © 2022. Published by Elsevier Inc.
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Snippet Metalloproteins represent a substantial fraction of the proteome where they have an outsized contribution to enzymology. This stems from the reactivity of...
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SubjectTerms Electronic structure
Metal homeostasis and trafficking
Metalloproteins
NMR spectroscopy
Paramagnetic
Structural biology
Title NMR of paramagnetic metalloproteins in solution: Ubi venire, quo vadis?
URI https://dx.doi.org/10.1016/j.jinorgbio.2022.111871
https://www.ncbi.nlm.nih.gov/pubmed/35636014
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