Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis

Nature ◽  
1990 ◽  
Vol 343 (6254) ◽  
pp. 188-190 ◽  
Author(s):  
Deborah J. Scott ◽  
Harold D. May ◽  
William E. Newton ◽  
Kevin E. Brigle ◽  
Dennis R. Dean
Keyword(s):  
Α Subunit ◽  
Cofactor Binding ◽  
Mofe Protein ◽  
Femo Cofactor

Role of the MoFe Protein .alpha.-Subunit Histidine-195 Residue in FeMo-cofactor Binding and Nitrogenase Catalysis

Biochemistry ◽  
1995 ◽  
Vol 34 (9) ◽  
pp. 2798-2808 ◽  
Author(s):  
Chul-Hwan Kim ◽  
William E. Newton ◽  
Dennis R. Dean
Keyword(s):  
Alpha Subunit ◽  
Cofactor Binding ◽  
Mofe Protein ◽  
Femo Cofactor ◽  
Protein Alpha Subunit

scholarly journals Nitrogenase MoFe protein fromClostridium pasteurianumat 1.08 Å resolution: comparison with theAzotobacter vinelandiiMoFe protein

2015 ◽  
Vol 71 (2) ◽  
pp. 274-282 ◽  
Author(s):  
Li-Mei Zhang ◽  
Christine N. Morrison ◽  
Jens T. Kaiser ◽  
Douglas C. Rees
Keyword(s):  
Active Sites ◽  
Azotobacter Vinelandii ◽  
Protein Structures ◽  
Protein Docking ◽  
Α Subunit ◽  
Mofe Protein ◽  
Fe Protein ◽  
Surrounding Environment ◽  
Solvent Environment ◽  
Femo Cofactor

The X-ray crystal structure of the nitrogenase MoFe protein fromClostridium pasteurianum(Cp1) has been determined at 1.08 Å resolution by multiwavelength anomalous diffraction phasing. Cp1 and the ortholog fromAzotobacter vinelandii(Av1) represent two distinct families of nitrogenases, differing primarily by a long insertion in the α-subunit and a deletion in the β-subunit of Cp1 relative to Av1. Comparison of these two MoFe protein structures at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase. The FeMo cofactors defining the active sites of the MoFe protein are essentially identical between the two proteins. The surrounding environment is also highly conserved, suggesting that this structural arrangement is crucial for nitrogen reduction. The P clusters are likewise similar, although the surrounding protein and solvent environment is less conserved relative to that of the FeMo cofactor. The P cluster and FeMo cofactor in Av1 and Cp1 are connected through a conserved water tunnel surrounded by similar secondary-structure elements. The long α-subunit insertion loop occludes the presumed Fe protein docking surface on Cp1 with few contacts to the remainder of the protein. This makes it plausible that this loop is repositioned to open up the Fe protein docking surface for complex formation.

scholarly journals Comment on “Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase”

Science ◽  
2021 ◽  
Vol 371 (6530) ◽  
pp. eabe5481 ◽  
Author(s):  
John W. Peters ◽  
Oliver Einsle ◽  
Dennis R. Dean ◽  
Serena DeBeer ◽  
Brian M. Hoffman ◽  
...  
Keyword(s):  
Active Site ◽  
Biochemical Evidence ◽  
Mofe Protein ◽  
Femo Cofactor

Kang et al. (Reports, 19 June 2020, p. 1381) report a structure of the nitrogenase MoFe protein that is interpreted to indicate binding of N2 or an N2-derived species to the active-site FeMo cofactor. Independent refinement of the structure and consideration of biochemical evidence do not support this claim.

scholarly journals Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements

2016 ◽  
Vol 56 (9-10) ◽  
pp. 841-851 ◽  
Author(s):  
Roman Davydov ◽  
Nimesh Khadka ◽  
Zhi-Yong Yang ◽  
Andrew J. Fielding ◽  
Dmitriy Lukoyanov ◽  
...  
Keyword(s):  
Proton Transfer ◽  
Conformational Changes ◽  
Mofe Protein ◽  
Femo Cofactor ◽  
Epr Measurements ◽  
Electron Proton Transfer

scholarly journals Nitrogenase from Klebsiella pneumoniae. An e.p.r. signal observed during enzyme turnover under ethylene is associated with the iron-molybdenum cofactor

1983 ◽  
Vol 211 (2) ◽  
pp. 495-497 ◽  
Author(s):  
T R Hawkes ◽  
D J Lowe ◽  
B E Smith
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Klebsiella Pneumoniae ◽  
Isotopic Substitution ◽  
Resonance Signal ◽  
Paramagnetic Resonance ◽  
Mofe Protein ◽  
Femo Cofactor ◽  
Enzyme Turnover ◽  
Iron Molybdenum Cofactor ◽  
Electron Paramagnetic

During turnover at 10 degrees C at pH 7.4 in the presence of ethylene, the MoFe protein of Klebsiella pneumoniae nitrogenase (Kp 1) exhibited an electron-paramagnetic-resonance signal with g-values at 2.12, 1.998 and 1.987. 57Fe isotopic substitution demonstrated that this signal arose from the Kp 1 FeMo-cofactor in an S = 1/2 spin state.

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