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

Fe protein-independent substrate reduction by nitrogenase MoFe protein variants.

Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding.

Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.

Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein.

The biosynthesis of nitrogenase MoFe protein polypeptides in free-living cultures of Rhizobium japonicum.

Nitrogenase: properties of the catalytically inactive complex between the Azotobacter vinelandii MoFe protein and the Clostridium pasteurianum Fe protein.

Nitrogenase XI: Mössbauer studies on the cofactor centers of the MoFe protein from Azotobacter vinelandii OP.

Turnover-dependent inactivation of the nitrogenase MoFe-protein at high pH.

EPR Measurements.

Altered nitrogenase MoFe proteins from Azotobacter vinelandii. Analysis of MoFe proteins having amino acid substitutions for the conserved cysteine residues within the beta-subunit.

Evidence for Functionally Relevant Encounter Complexes in Nitrogenase Catalysis.

Nitrogen fixation and bioenergetics: the role of ATP in nitrogenase catalysis.

Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP. Nature of the iron centers.

Low frequency dynamics of the nitrogenase MoFe protein via femtosecond pump probe spectroscopy - Observation of a candidate promoting vibration.

Evidence that conserved residues Cys-62 and Cys-154 within the Azotobacter vinelandii nitrogenase MoFe protein α-subunit are essential for nitrogenase activity but conserved residues His-83 and Cys-88 are not.

Nonenzymatic synthesis of the P-cluster in the nitrogenase MoFe protein: evidence of the involvement of all-ferrous [Fe4S4](0) intermediates.

Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor.

Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125.

Ethylene Glycol Quenching of Nitrogenase Catalysis: An Electron Paramagnetic Resonance Spectroscopic Study of Nitrogenase Turnover States and CO Bonding.

Binding energy and enzymic catalysis.

Klebsiella pneumoniae nitrogenase. The pre-steady-state kinetics of MoFe-protein reduction and hydrogen evolution under conditions of limiting electron flux show that the rates of association with the Fe-protein and electron transfer are independent of the oxidation level of the MoFe-protein.

Negative cooperativity in the nitrogenase Fe protein electron delivery cycle.

The role of snRNAs in spliceosomal catalysis.

Protein dynamics and the all-ferrous [Fe4 S4 ] cluster in the nitrogenase iron protein.

Suggest Documents

Fe protein-independent substrate reduction by nitrogenase MoFe protein variants.

Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding.

Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.

Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein.

The biosynthesis of nitrogenase MoFe protein polypeptides in free-living cultures of Rhizobium japonicum.

Nitrogenase: properties of the catalytically inactive complex between the Azotobacter vinelandii MoFe protein and the Clostridium pasteurianum Fe protein.

Nitrogenase XI: Mössbauer studies on the cofactor centers of the MoFe protein from Azotobacter vinelandii OP.

Turnover-dependent inactivation of the nitrogenase MoFe-protein at high pH.

EPR Measurements.

Altered nitrogenase MoFe proteins from Azotobacter vinelandii. Analysis of MoFe proteins having amino acid substitutions for the conserved cysteine residues within the beta-subunit.

Evidence for Functionally Relevant Encounter Complexes in Nitrogenase Catalysis.

Nitrogen fixation and bioenergetics: the role of ATP in nitrogenase catalysis.

Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP. Nature of the iron centers.

Low frequency dynamics of the nitrogenase MoFe protein via femtosecond pump probe spectroscopy - Observation of a candidate promoting vibration.

Evidence that conserved residues Cys-62 and Cys-154 within the Azotobacter vinelandii nitrogenase MoFe protein α-subunit are essential for nitrogenase activity but conserved residues His-83 and Cys-88 are not.

Nonenzymatic synthesis of the P-cluster in the nitrogenase MoFe protein: evidence of the involvement of all-ferrous [Fe4S4](0) intermediates.

Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor.

Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125.

Ethylene Glycol Quenching of Nitrogenase Catalysis: An Electron Paramagnetic Resonance Spectroscopic Study of Nitrogenase Turnover States and CO Bonding.

Binding energy and enzymic catalysis.

Klebsiella pneumoniae nitrogenase. The pre-steady-state kinetics of MoFe-protein reduction and hydrogen evolution under conditions of limiting electron flux show that the rates of association with the Fe-protein and electron transfer are independent of the oxidation level of the MoFe-protein.

Negative cooperativity in the nitrogenase Fe protein electron delivery cycle.

The role of snRNAs in spliceosomal catalysis.

Protein dynamics and the all-ferrous [Fe4 S4 ] cluster in the nitrogenase iron protein.

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

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