Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N 2 Reduction

Shaw, Sudipta; Lukoyanov, Dmitriy; Danyal, Karamatullah; Dean, Dennis R.; Hoffman, Brian M.; Seefeldt, Lance C.

doi:10.1021/ja507123d

Title: Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N ₂ Reduction

Full Record
Other Related Research

Authors:

Shaw, Sudipta ^[1]; Lukoyanov, Dmitriy ^[2]; Danyal, Karamatullah ^[1]; Dean, Dennis R. ^[3]; Hoffman, Brian M. ^[2]; Seefeldt, Lance C. ^[1]

Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, United States
Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States
Department of Biochemistry, Virginia Tech, 110 Fralin Hall, Blacksburg, Virginia 24061, United States

Publication Date:: Thu Aug 28 00:00:00 EDT 2014

Sponsoring Org.:: USDOE

OSTI Identifier:: 1158725

Grant/Contract Number:: SC0010687

Resource Type:: Published Article

Journal Name:: Journal of the American Chemical Society

Additional Journal Information:: Journal Name: Journal of the American Chemical Society Journal Volume: 136 Journal Issue: 36; Journal ID: ISSN 0002-7863

Publisher:: American Chemical Society

Country of Publication:: United States

Language:: English

Citation Formats


                    Shaw, Sudipta, Lukoyanov, Dmitriy, Danyal, Karamatullah, Dean, Dennis R., Hoffman, Brian M., and Seefeldt, Lance C. Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N 2 Reduction.  United States: N. p., 2014. 
Web.  doi:10.1021/ja507123d.

Copy to clipboard


                    Shaw, Sudipta, Lukoyanov, Dmitriy, Danyal, Karamatullah, Dean, Dennis R., Hoffman, Brian M., & Seefeldt, Lance C. Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N 2 Reduction.  United States.  https://doi.org/10.1021/ja507123d

Copy to clipboard


                    Shaw, Sudipta, Lukoyanov, Dmitriy, Danyal, Karamatullah, Dean, Dennis R., Hoffman, Brian M., and Seefeldt, Lance C. Thu .  
"Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N 2 Reduction".  United States.  https://doi.org/10.1021/ja507123d.

Copy to clipboard


                    
@article{osti_1158725,

  title        = {Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N 2 Reduction},

  author       = {Shaw, Sudipta and Lukoyanov, Dmitriy and Danyal, Karamatullah and Dean, Dennis R. and Hoffman, Brian M. and Seefeldt, Lance C.},

  abstractNote = {},

  doi          = {10.1021/ja507123d},

  journal      = {Journal of the American Chemical Society},

  number       = 36,

  volume       = 136,

  place        = {United States},

  year         = {Thu Aug 28 00:00:00 EDT 2014},

  month        = {Thu Aug 28 00:00:00 EDT 2014}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1021/ja507123d

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 30 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

CO₂ Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane

Journal Article Khadka, Nimesh ; Dean, Dennis R. ; Smith, Dayle ; ... - Inorganic Chemistry

The reduction of N₂ to NH₃ by Mo-dependent nitrogenase at its active-site metal cluster FeMo-cofactor utilizes reductive elimination (re) of Fe-bound hydrides with obligatory loss of H₂ to activate the enzyme for binding/reduction of N₂. Earlier work showed that wild type nitrogenase and a nitrogenase having amino acid substitutions in the MoFe protein near FeMo-cofactor can catalytically reduce CO₂ by 2 or 8 electrons/protons to carbon monoxide (CO) and methane (CH₄) at low rates. Here, it is demonstrated that nitrogenase preferentially reduces CO₂ by 2 electrons/protons to formate (HCOO^–) at rates >10 times higher than rates of CO₂ reduction tomore »« less
Cited by 33
https://doi.org/10.1021/acs.inorgchem.6b00388

Full Text Available
Reductive Elimination of H₂ Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E₄(4H) Janus Intermediate in Wild-Type Enzyme

Journal Article Lukoyanov, Dmitriy ; Khadka, Nimesh ; Yang, Zhi -Yong ; ... - Journal of the American Chemical Society

Here, we have proposed a reductive elimination/oxidative addition (re/oa) mechanism for reduction of N₂ to 2NH₃ by nitrogenase, based on identification of a freeze-trapped intermediate of the α-70^Val→Ile substituted MoFe protein as the Janus intermediate that stores four reducing equivalents on FeMo-co as two [Fe-H-Fe] bridging hydrides (denoted E₄(4H)). The mechanism postulates that obligatory re of the hydrides as H₂ drives reduction of N₂ to a state (denoted E₄(2N2H)) with a moiety at the diazene (HN=NH) reduction level bound to the catalytic FeMo-cofactor. In the present work, EPR/ENDOR and photophysical measurements show that a state freeze-trapped during N₂ reduction bymore »« less
Cited by 107
https://doi.org/10.1021/jacs.6b06362

Full Text Available
Kinetic Understanding of N ₂ Reduction versus H ₂ Evolution at the E ₄ (4H) Janus State in the Three Nitrogenases

Journal Article Harris, Derek F. ; Yang, Zhi-Yong ; Dean, Dennis R. ; ... - Biochemistry

Not provided.
https://doi.org/10.1021/acs.biochem.8b00784
Mo-, V-, and Fe-Nitrogenases Use a Universal Eight-Electron Reductive-Elimination Mechanism To Achieve N ₂ Reduction

Journal Article Harris, Derek F. ; Lukoyanov, Dmitriy A. ; Kallas, Hayden ; ... - Biochemistry

Not provided.
https://doi.org/10.1021/acs.biochem.9b00468
Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for N ₂ reduction

Journal Article Raugei, Simone ; Seefeldt, Lance C. ; Hoffman, Brian M. - Proceedings of the National Academy of Sciences of the United States of America

Recent spectroscopic, kinetic, photophysical, and thermodynamic measurements show activation of nitrogenase for N₂→ 2NH₃ reduction involves the reductive elimination (re) of H₂from two [Fe–H–Fe] bridging hydrides bound to the catalytic [7Fe–9S–Mo–C–homocitrate] FeMo-cofactor (FeMo-co). These studies rationalize the Lowe–Thorneley kinetic scheme’s proposal of mechanistically obligatory formation of one H₂for each N₂reduced. They also provide an overall framework for understanding the mechanism of nitrogen fixation by nitrogenase. However, they directly pose fundamental questions addressed computationally here. We here report an extensive computational investigation of the structure and energetics of possible nitrogenase intermediates using structural models for the active site with a broadmore »« less
Cited by 88
https://doi.org/10.1073/pnas.1810211115

Similar Records

Title: Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N 2 Reduction

Citation Formats

Title: Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N ₂ Reduction