N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation. - Wikidata - awgldk - TriplyDB

N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.

N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.

http://www.wikidata.org/entity/Q37557969

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Mechanism of nitrogen fixation by nitrogenase: the next stage Controlled protonation of iron-molybdenum cofactor by nitrogenase: a structural and theoretical analysis Mechanism of Mo-dependent nitrogenase Dual functions of NifEN: insights into the evolution and mechanism of nitrogenase.

P2860

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P2860

N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.

http://www.wikidata.org/entity/Q37557969

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on August 1991

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

N coordination of FeMo cofacto ...... biological nitrogen fixation.

@en

N coordination of FeMo cofacto ...... biological nitrogen fixation.

@nl

type

label

N coordination of FeMo cofacto ...... biological nitrogen fixation.

@en

N coordination of FeMo cofacto ...... biological nitrogen fixation.

@nl

prefLabel

N coordination of FeMo cofacto ...... biological nitrogen fixation.

@en

N coordination of FeMo cofacto ...... biological nitrogen fixation.

@nl

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PNAS.88.15.6620

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

N coordination of FeMo cofacto ...... biological nitrogen fixation.

@en

P2093

Bernardo M

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Dean DR

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Newton WE

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Thomann H

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P2860

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

Isolation of an iron-molybdenum cofactor from nitrogenase.

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

Novel metal cluster in the iron-molybdenum cofactor of nitrogenase. Spectroscopic evidence.

Nitrogenase from nifV mutants of Klebsiella pneumoniae contains an altered form of the iron-molybdenum cofactor.

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

Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster.

P304

6620-6623

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scholarly article

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10.1073/PNAS.88.15.6620

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15

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P478

88

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1991-08-01T00:00:00Z

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11743768

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11607203

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52139

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