Role of PsbV-Tyr137 in photosystem II studied by site-directed mutagenesis in the thermophilic cyanobacterium Thermosynechococcus vulcanus

Directed Mutagenesis ◽

Thermophilic Cyanobacterium

Site-Directed Mutagenesis to Probe the Role of the D2 Protein in Photosystem II

Regulation of Chloroplast Biogenesis ◽

10.1007/978-1-4615-3366-5_82 ◽

1992 ◽

pp. 567-574

Author(s):

Beth Eggers ◽

Wim Vermaas

Keyword(s):

Photosystem Ii ◽

Directed Mutagenesis ◽

D2 Protein

Using site-directed mutagenesis to probe the role of the D2 carotenoid in the secondary electron-transfer pathway of photosystem II

Photosynthesis Research ◽

10.1007/s11120-013-9793-6 ◽

2013 ◽

Vol 120 (1-2) ◽

pp. 141-152 ◽

Cited By ~ 8

Author(s):

Katherine E. Shinopoulos ◽

Jianfeng Yu ◽

Peter J. Nixon ◽

Gary W. Brudvig

Keyword(s):

Electron Transfer ◽

Photosystem Ii ◽

Secondary Electron ◽

Directed Mutagenesis ◽

Electron Transfer Pathway

Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase

10.1016/s0021-9258(19)67801-4 ◽

1991 ◽

Vol 266 (6) ◽

pp. 3372-3375

Author(s):

T Shimizu ◽

T Tateishi ◽

M Hatano ◽

Y Fujii-Kuriyama

Keyword(s):

Cytochrome P450 ◽

Directed Mutagenesis ◽

Cytochrome P450 Reductase ◽

Nadph Cytochrome ◽

P450 Reductase ◽

Catalytic Function ◽

Nadph Cytochrome P450 Reductase

The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR.

10.1016/s0021-9258(18)54766-9 ◽

1991 ◽

Vol 266 (31) ◽

pp. 20709-20713

Author(s):

L.J. Donald ◽

B.R. Crane ◽

D.H. Anderson ◽

H.W. Duckworth

Keyword(s):

Escherichia Coli ◽

Chemical Modification ◽

Citrate Synthase ◽

19F Nmr ◽

Directed Mutagenesis ◽

Allosteric Inhibition

Role of Cysteine Residues in the N-Terminal Extracellular Domain of the Human VIP 1 Receptor for Ligand Binding A Site-directed Mutagenesis Studya

Annals of the New York Academy of Sciences ◽

10.1111/j.1749-6632.1996.tb17524.x ◽

2006 ◽

Vol 805 (1) ◽

pp. 585-589 ◽

Cited By ~ 4

Author(s):

PASCALE GAUDIN ◽

ALAIN COUVINEAU ◽

JEAN-JOSÉ MAORET ◽

CHRISTIANE ROUYER-FESSARD ◽

MARC LABURTHE

Keyword(s):

Ligand Binding ◽

Extracellular Domain ◽

Cysteine Residues ◽

Directed Mutagenesis ◽

A Site

Site-directed mutagenesis of tyrosine hydroxylase. Role of serine 40 in catalysis.

10.1016/s0021-9258(18)35673-4 ◽

1992 ◽

Vol 267 (36) ◽

pp. 25754-25758

Author(s):

J Wu ◽

D Filer ◽

A.J. Friedhoff ◽

M Goldstein

Keyword(s):

Tyrosine Hydroxylase ◽

Directed Mutagenesis

Determination of the functional role of phenylalanine-31 of recombinant human dihydrofolate reductase by site-directed mutagenesis

Zurich, Switzerland, September 3–8, 1989 ◽

10.1515/9783110889000-148 ◽

1990 ◽

pp. 765-768

Keyword(s):

Dihydrofolate Reductase ◽

Functional Role ◽

Directed Mutagenesis ◽

Human Dihydrofolate Reductase

The role of cysteines in polyketide synthases. Site-directed mutagenesis of resveratrol and chalcone synthases, two key enzymes in different plant-specific pathways

10.1016/s0021-9258(18)92914-5 ◽

1991 ◽

Vol 266 (15) ◽

pp. 9971-9976 ◽

Cited By ~ 3

Author(s):

T. Lanz ◽

S. Tropf ◽

F.J. Marner ◽

J. Schröder ◽

G. Schröder

Keyword(s):

Polyketide Synthases ◽

Directed Mutagenesis ◽

Key Enzymes

The role of Val68(E11) in ligand binding to sperm whale myoglobin. Site-directed mutagenesis of a synthetic gene.

10.1016/s0021-9258(19)38467-4 ◽

1990 ◽

Vol 265 (20) ◽

pp. 11788-11795

Author(s):

K D Egeberg ◽

B A Springer ◽

S G Sligar ◽

T E Carver ◽

R J Rohlfs ◽

...

Keyword(s):

Ligand Binding ◽

Sperm Whale ◽

Synthetic Gene ◽

Directed Mutagenesis ◽

Sperm Whale Myoglobin

Probing the Role of Tyr 64 ofTreponema denticolaCystalysin by Site-Directed Mutagenesis and Kinetic Studies†

Biochemistry ◽

10.1021/bi051433n ◽

2005 ◽

Vol 44 (42) ◽

pp. 13970-13980 ◽

Cited By ~ 17

Author(s):

Barbara Cellini ◽

Mariarita Bertoldi ◽

Riccardo Montioli ◽

Carla Borri Voltattorni

Keyword(s):

Kinetic Studies ◽

Directed Mutagenesis