Covalent modification of nitrogenase MoFe protein by ADP.

Item

http://www.wikidata.org/entity/Q42985914

description

1997 nî lūn-bûn

@nan

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

1997年论文

@zh

1997年论文

@zh-cn

name

Covalent modification of nitrogenase MoFe protein by ADP.

@en

Covalent modification of nitrogenase MoFe protein by ADP.

@nl

type

Item

label

Covalent modification of nitrogenase MoFe protein by ADP.

@en

Covalent modification of nitrogenase MoFe protein by ADP.

@nl

prefLabel

Covalent modification of nitrogenase MoFe protein by ADP.

@en

Covalent modification of nitrogenase MoFe protein by ADP.

@nl

P1476

Covalent modification of nitrogenase MoFe protein by ADP.

@en

P2093

Eady RR

http://www.w3.org/2001/XMLSchema#string

Fairhurst SA

http://www.w3.org/2001/XMLSchema#string

Gormal C

http://www.w3.org/2001/XMLSchema#string

Miller RW

http://www.w3.org/2001/XMLSchema#string

Smith BE

http://www.w3.org/2001/XMLSchema#string

P2860

Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii.

Nitrogenase and biological nitrogen fixation.

Evidence on the role(s) of ATP in the mechanism of nitrogenase, from proton NMR relaxation studies on metal and nucleotide binding to the molybdenum-iron protein.

Nitrogenase: a nucleotide-dependent molecular switch.

Isolation and characterization of nitrogenase MoFe protein from the mutant strain pHK17 of Klebsiella pneumoniae in which the two bridging cysteine residues of the P-clusters are replaced by the non-coordinating amino acid alanine.

Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins.

Increasing nitrogenase catalytic efficiency for MgATP by changing serine 16 of its Fe protein to threonine: use of Mn2+ to show interaction of serine 16 with Mg2+.

Energy transduction by nitrogenase: binding of MgADP to the MoFe protein is dependent on the oxidation state of the iron-sulphur 'P' clusters.

A transient-kinetic study of the nitrogenase of Klebsiella pneumoniae by stopped-flow calorimetry. Comparison with the myosin ATPase.

Nitrogenase of Klebsiella pneumoniae. Kinetics of the dissociation of oxidized iron protein from molybdenum-iron protein: identification of the rate-limiting step for substrate reduction.

P304

737-744

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1042/BJ3220737

http://www.w3.org/2001/XMLSchema#string

P407

English

P478

322 ( Pt 3)

http://www.w3.org/2001/XMLSchema#string

P577

1997-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

14069295

http://www.w3.org/2001/XMLSchema#string

P698

9148743

http://www.w3.org/2001/XMLSchema#string

P932

1218249

http://www.w3.org/2001/XMLSchema#string