EXAFS studies of FeMo-cofactor and MoFe protein: Direct evidence for the long-range Mo-Fe-Fe interaction and cyanide binding to the Mo in FeMo-cofactor

1994 ◽  
Vol 116 (6) ◽  
pp. 2418-2423 ◽  
Author(s):  
Hongbin Isaac Liu ◽  
Barbara K. Burgess ◽  
Calogero R. Natoli ◽  
Adriano Filipponi ◽  
Narasaiah Gavini ◽  
...  
Keyword(s):  
Long Range ◽  
Direct Evidence ◽  
Mofe Protein ◽  
Cyanide Binding ◽  
Femo Cofactor

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.

Kinetic and theoretical studies of cyanide binding to the extracted FeMo-cofactor of nitrogenase

2003 ◽  
Vol 96 (1) ◽  
pp. 232
Author(s):  
Barry E. Smith ◽  
Zhen Cui ◽  
Adrian J. Dunford ◽  
Marcus C. Durrant ◽  
Richard A. Henderson
Keyword(s):  
Theoretical Studies ◽  
Cyanide Binding ◽  
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 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.

Site-specific mutations of the nitrogenase MoFe protein: ESEEM and ENDOR spectroscopic analyses of amino acid substitutions near to the FeMo-cofactor

1995 ◽  
Vol 59 (2-3) ◽  
pp. 550
Author(s):  
Victoria J. DeRose ◽  
Chul-Hwan Kim ◽  
John W. Peters ◽  
William E. Newton ◽  
Dennis R. Dean ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitutions ◽  
Site Specific ◽  
Mofe Protein ◽  
Spectroscopic Analyses ◽  
Femo Cofactor
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