Reactivity, Mechanism, and Assembly of the Alternative Nitrogenases

Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated with the molybdenum–iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural...

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Bibliographic Details
Published inChemical reviews Vol. 120; no. 12; pp. 5107 - 5157
Main Authors Jasniewski, Andrew J, Lee, Chi Chung, Ribbe, Markus W, Hu, Yilin
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 24.06.2020
Subjects
biosynthesis
catalytic activity
chemical bonding
Chemistry
Cluster chemistry
Crystal structure
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Iron
Models, Molecular
Molybdenum
Molybdenum - chemistry
Molybdenum - metabolism
Monomers
multigene family
Nitrogen
Nitrogen - chemistry
Nitrogen - metabolism
Nitrogen Fixation
nitrogenase
Nitrogenase - chemistry
Nitrogenase - metabolism
Nitrogenation
Peptides and proteins
spectral analysis
Structural analysis
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Abstract Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated with the molybdenum–iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural and spectroscopic characterization over the past 60 years. In the late 1980s and early 1990s, two “alternative nitrogenase” systems were discovered, isolated, and found to incorporate V or Fe in place of Mo. These systems are regulated by separate gene clusters; however, there is a high degree of structural and functional similarity between each nitrogenase. Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found capabilities that are unique to the alternative systems. In this review, we will discuss the reactivity, biosynthetic, and mechanistic proposals for the alternative nitrogenases as well as their electronic and structural properties in comparison to the well-characterized Mo-dependent system. Studies over the past 10 years have been particularly fruitful, though key aspects about V- and Fe-nitrogenases remain unexplored.
AbstractList Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated with the molybdenum-iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural and spectroscopic characterization over the past 60 years. In the late 1980s and early 1990s, two "alternative nitrogenase" systems were discovered, isolated, and found to incorporate V or Fe in place of Mo. These systems are regulated by separate gene clusters; however, there is a high degree of structural and functional similarity between each nitrogenase. Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found capabilities that are unique to the alternative systems. In this review, we will discuss the reactivity, biosynthetic, and mechanistic proposals for the alternative nitrogenases as well as their electronic and structural properties in comparison to the well-characterized Mo-dependent system. Studies over the past 10 years have been particularly fruitful, though key aspects about V- and Fe-nitrogenases remain unexplored.Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated with the molybdenum-iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural and spectroscopic characterization over the past 60 years. In the late 1980s and early 1990s, two "alternative nitrogenase" systems were discovered, isolated, and found to incorporate V or Fe in place of Mo. These systems are regulated by separate gene clusters; however, there is a high degree of structural and functional similarity between each nitrogenase. Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found capabilities that are unique to the alternative systems. In this review, we will discuss the reactivity, biosynthetic, and mechanistic proposals for the alternative nitrogenases as well as their electronic and structural properties in comparison to the well-characterized Mo-dependent system. Studies over the past 10 years have been particularly fruitful, though key aspects about V- and Fe-nitrogenases remain unexplored.
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated with the molybdenum–iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural and spectroscopic characterization over the past 60 years. In the late 1980s and early 1990s, two "alternative nitrogenase" systems were discovered, isolated, and found to incorporate V or Fe in place of Mo. These systems are regulated by separate gene clusters; however, there is a high degree of structural and functional similarity between each nitrogenase. Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found capabilities that are unique to the alternative systems. In this review, we will discuss the reactivity, biosynthetic, and mechanistic proposals for the alternative nitrogenases as well as their electronic and structural properties in comparison to the well-characterized Mo-dependent system. Studies over the past 10 years have been particularly fruitful, though key aspects about V- and Fe-nitrogenases remain unexplored.
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N . Nitrogenase is most commonly associated with the molybdenum-iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural and spectroscopic characterization over the past 60 years. In the late 1980s and early 1990s, two "alternative nitrogenase" systems were discovered, isolated, and found to incorporate V or Fe in place of Mo. These systems are regulated by separate gene clusters; however, there is a high degree of structural and functional similarity between each nitrogenase. Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found capabilities that are unique to the alternative systems. In this review, we will discuss the reactivity, biosynthetic, and mechanistic proposals for the alternative nitrogenases as well as their electronic and structural properties in comparison to the well-characterized Mo-dependent system. Studies over the past 10 years have been particularly fruitful, though key aspects about V- and Fe-nitrogenases remain unexplored.
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N₂. Nitrogenase is most commonly associated with the molybdenum–iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural and spectroscopic characterization over the past 60 years. In the late 1980s and early 1990s, two “alternative nitrogenase” systems were discovered, isolated, and found to incorporate V or Fe in place of Mo. These systems are regulated by separate gene clusters; however, there is a high degree of structural and functional similarity between each nitrogenase. Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found capabilities that are unique to the alternative systems. In this review, we will discuss the reactivity, biosynthetic, and mechanistic proposals for the alternative nitrogenases as well as their electronic and structural properties in comparison to the well-characterized Mo-dependent system. Studies over the past 10 years have been particularly fruitful, though key aspects about V- and Fe-nitrogenases remain unexplored.
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N 2 . Nitrogenase is most commonly associated with the molybdenum-iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural and spectroscopic characterization over the past 60 years. In the late 1980’s and early 1990’s, two ‘alternative nitrogenase’ systems were discovered, isolated, and were found to incorporate V or Fe in place of the Mo. These systems are regulated by separate gene clusters, however, there is a high degree of structural and functional similarity between each nitrogenase. Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found capabilities that are unique to the alternative systems. In this review, we will discuss the reactivity, biosynthetic and mechanistic proposals for the alternative nitrogenases as well as their electronic and structural properties in comparison to the well-characterized Mo-dependent system. Studies over the past 10 years have been particularly fruitful, though, key aspects about V- and Fe-nitrogenases remain unexplored.
Author Hu, Yilin
Jasniewski, Andrew J
Lee, Chi Chung
Ribbe, Markus W
AuthorAffiliation Department of Chemistry
University of California
Department of Molecular Biology and Biochemistry
AuthorAffiliation_xml – name: Department of Molecular Biology and Biochemistry
– name: University of California
– name: Department of Chemistry
– name: a Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900
– name: b Department of Chemistry, University of California, Irvine, CA 92697-2025
Author_xml – sequence: 1
  givenname: Andrew J
  orcidid: 0000-0001-7614-0796
  surname: Jasniewski
  fullname: Jasniewski, Andrew J
  organization: Department of Molecular Biology and Biochemistry
– sequence: 2
  givenname: Chi Chung
  surname: Lee
  fullname: Lee, Chi Chung
  organization: Department of Molecular Biology and Biochemistry
– sequence: 3
  givenname: Markus W
  orcidid: 0000-0002-7366-1526
  surname: Ribbe
  fullname: Ribbe, Markus W
  email: mribbe@uci.edu
  organization: University of California
– sequence: 4
  givenname: Yilin
  orcidid: 0000-0002-9088-2865
  surname: Hu
  fullname: Hu, Yilin
  email: yilinh@uci.edu
  organization: Department of Molecular Biology and Biochemistry
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32129988$$D View this record in MEDLINE/PubMed
https://www.osti.gov/servlets/purl/1802675$$D View this record in Osti.gov
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SSID ssj0005527
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SecondaryResourceType review_article
Snippet Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N2. Nitrogenase is...
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N . Nitrogenase is...
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N₂. Nitrogenase is...
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N 2 . Nitrogenase is...
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osti
proquest
pubmed
crossref
acs
SourceType Open Access Repository
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Index Database
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Publisher
StartPage 5107
SubjectTerms biosynthesis
catalytic activity
chemical bonding
Chemistry
Cluster chemistry
Crystal structure
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Iron
Models, Molecular
Molybdenum
Molybdenum - chemistry
Molybdenum - metabolism
Monomers
multigene family
Nitrogen
Nitrogen - chemistry
Nitrogen - metabolism
Nitrogen Fixation
nitrogenase
Nitrogenase - chemistry
Nitrogenase - metabolism
Nitrogenation
Peptides and proteins
spectral analysis
Structural analysis
Title Reactivity, Mechanism, and Assembly of the Alternative Nitrogenases
URI http://dx.doi.org/10.1021/acs.chemrev.9b00704
https://www.ncbi.nlm.nih.gov/pubmed/32129988
https://www.proquest.com/docview/2417479297
https://www.proquest.com/docview/2371861413
https://www.proquest.com/docview/2439428869
https://www.osti.gov/servlets/purl/1802675
https://pubmed.ncbi.nlm.nih.gov/PMC7491575
Volume 120
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