Functional and Structural Model for the Molybdenum-Pterin Binding Site in Dimethyl Sulfoxide Reductase. Synthesis, Crystal Structure, and Spectroscopic Investigations of Trichloro(quinoid-N(8)H-6,7-dihydropterin)oxomolybdenum(IV)

1995 ◽  
Vol 34 (23) ◽  
pp. 5726-5734 ◽  
Author(s):  
Berthold Fischer ◽  
Helmut Schmalle ◽  
Erich Dubler ◽  
Andrea Schaefer ◽  
Max Viscontini
Keyword(s):  
Crystal Structure ◽  
Dimethyl Sulfoxide ◽  
Binding Site ◽  
Structural Model ◽  
Spectroscopic Investigations ◽  
Dimethyl Sulfoxide Reductase

Crystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å Resolution

1996 ◽  
Vol 263 (1) ◽  
pp. 53-69 ◽  
Author(s):  
Frank Schneider ◽  
Jan Löwe ◽  
Robert Huber ◽  
Hermann Schindelin ◽  
Caroline Kisker ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dimethyl Sulfoxide ◽  
Dimethyl Sulfoxide Reductase

scholarly journals Crystal structure of 2,4,7,9-tetranitro-10H-benzofuro[3,2-b]indole – dimethyl sulfoxide (1/1), C16H11N5O10S

2021 ◽  
Vol 236 (3) ◽  
pp. 523-525
Author(s):  
Huizhi Cao ◽  
Mi Yan ◽  
Shiliang Huang ◽  
Xuan He ◽  
Xiong Cao
Keyword(s):  
Crystal Structure ◽  
Dimethyl Sulfoxide

Abstract C16H11N5O10S, triclinic, P 1 ‾ $P‾{1}$ (no. 2), a = 4.6658(1) Å, b = 12.2129(4) Å, c = 17.0355(5) Å, α = 74.925(2)°, β = 86.398(2)°, γ $\gamma $  = 88.040(2)°, V = 935.31(5) Å3, Z = 2, R gt (F) = 0.0642, wR ref (F 2) = 0.1744, T = 295 K.

scholarly journals The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide.

1984 ◽  
Vol 259 (5) ◽  
pp. 2822-2825 ◽  
Author(s):  
T P Garrett ◽  
D J Clingeleffer ◽  
J M Guss ◽  
S J Rogers ◽  
H C Freeman
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Copper Binding

The crystal structure of (Z)-3-hydrazono-5-nitroindolin-2-one – dimethyl sulfoxide (1/1), C8H6N4O3

2020 ◽  
Vol 235 (2) ◽  
pp. 501-502
Author(s):  
Abdulrahman M. Al-Obaid ◽  
Saeed Ali Syed ◽  
Bari Ahmed ◽  
Eric C. Hosten
Keyword(s):  
Crystal Structure ◽  
Dimethyl Sulfoxide

AbstractC8H6N4O3 ⋅ C2H6OS, orthorhombic, Pnma (no. 62), a = 10.4813(5) Å, b = 6.8663(4) Å, c = 17.2605(9) Å, V = 1242.20(11) Å3, Z = 4, Rgt(F) = 0.0506, wRref(F2) = 0.1590, T = 200(2) K.

scholarly journals Characterization of the Acetate Binding Pocket in the Methanosarcina thermophila Acetate Kinase

2005 ◽  
Vol 187 (7) ◽  
pp. 2386-2394 ◽  
Author(s):  
Cheryl Ingram-Smith ◽  
Andrea Gorrell ◽  
Sarah H. Lawrence ◽  
Prabha Iyer ◽  
Kerry Smith ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Binding Pocket ◽  
Acetate Kinase ◽  
Phosphoryl Group ◽  
Acetyl Phosphate ◽  
Hydrophobic Pocket ◽  
Methanosarcina Thermophila ◽  
Methyl Group ◽  
Substrate Binding Sites

ABSTRACT Acetate kinase catalyzes the reversible magnesium-dependent synthesis of acetyl phosphate by transfer of the ATP γ-phosphoryl group to acetate. Inspection of the crystal structure of the Methanosarcina thermophila enzyme containing only ADP revealed a solvent-accessible hydrophobic pocket formed by residues Val93, Leu122, Phe179, and Pro232 in the active site cleft, which identified a potential acetate binding site. The hypothesis that this was a binding site was further supported by alignment of all acetate kinase sequences available from databases, which showed strict conservation of all four residues, and the recent crystal structure of the M. thermophila enzyme with acetate bound in this pocket. Replacement of each residue in the pocket produced variants with Km values for acetate that were 7- to 26-fold greater than that of the wild type, and perturbations of this binding pocket also altered the specificity for longer-chain carboxylic acids and acetyl phosphate. The kinetic analyses of variants combined with structural modeling indicated that the pocket has roles in binding the methyl group of acetate, influencing substrate specificity, and orienting the carboxyl group. The kinetic analyses also indicated that binding of acetyl phosphate is more dependent on interactions of the phosphate group with an unidentified residue than on interactions between the methyl group and the hydrophobic pocket. The analyses also indicated that Phe179 is essential for catalysis, possibly for domain closure. Alignments of acetate kinase, propionate kinase, and butyrate kinase sequences obtained from databases suggested that these enzymes have similar catalytic mechanisms and carboxylic acid substrate binding sites.

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