In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?

Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreductase (Ntr) domain. No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity.

{2-[(2-Acetyl-hydrazin-1-yl-idene)methyl-κN,O]-6-methoxy-phenolato-κO}(nitrato-κO)copper(II) monohydrate.

In the title complex, [Cu(C(10)H(11)N(2)O(3))(NO(3))]·H(2)O, prepared from the Schiff base N'-(3-meth-oxy-2-oxidobenzyl-idene)-acetohydrazide, the Cu(II) atom is coordinated by two O atoms and one N atom from the ligand and one O atom from a nitrate group in a distorted square-planar geometry. The Cu(II) atom has a weak inter-action with another O atom of the nitrate group. The two O atoms of the tridentate Schiff base ligand are in a trans arrangement.

Recombinant plant gamma carbonic anhydrase homotrimers bind inorganic carbon.

Gamma carbonic anhydrases (gammaCA) are widespread in Prokaryotes. In Eukaryotes, homologous genes were found only in plant genomes. In Arabidopsis and maize, the corresponding gene products are subunits of mitochondrial Complex I.

Bis(benzohydrazide-κO,N')bis-(nitrato-κO)copper(II).

In the title compound, [Cu(NO(3))(2)(C(7)H(8)N(2)O)(2)], the Cu(II) atom is located on a centre of inversion, and is coordinated by two bidentate benzohydrazide ligands and two monodentate nitrate anions in an axially distorted octa-hedral geometry within an N(2)O(4) donor set. The crystal structure is stabilized by N-H⋯O and weak N-H⋯N hydrogen bonds.

Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein from Thermotoga maritima.

Thermotoga maritima contains a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus. The peroxiredoxin (Prx) domain has been overproduced and purified from Escherichia coli cells. The recombinant Prx domain, which is homologous to bacterial Prx BCP and plant Prx Q, folds properly into a stable protein that possesses biological activity.

Structure-function analysis of the antiangiogenic ATWLPPR peptide inhibiting VEGF(165) binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex.

Heptapeptide ATWLPPR (A7R), identified in our laboratory by screening a mutated phage library, was shown to bind specifically to neuropilin-1 (NRP-1) and then to selectively inhibit VEGF(165) binding to this receptor. In vivo, treatment with A7R resulted in decreasing breast cancer angiogenesis and growth. The present work is focused on structural characterization of A7R.

Helical aquatubes of calix[4]arene di-methoxycarboxylic acid.

Two trimeric units of calix[4]arene di-methoxycarboxylic acid form a six-pointed star architecture that, in turn, generates triple helical aquatubes which intermesh between themselves by aromatic-aromatic interdigitation of the macrocycle.

A new packing motif for para-sulfonatocalix[4]arene: the solid state structure of the para-sulfonatocalix[4]arene D-arginine complex.

The solid-state structure of the complex of para-sulfonatocalix[4]arene with d-arginine, contains a water channel diagonal to a zigzag bilayer of the host, within the bilayer six crystallographically independent molecules of arginine are present, four being included in the calix cavities.

Solid-state caging of 1,10-phenanthroline pi-pi stacked dimers by calix[4]arene dihydroxyphosphonic acid.

The calix[4]arene dihydroxyphosphonic acid-1,10-phenanthroline complex shows caging of the guest molecules as a pi-pi stacked dimer in a cavity formed by intermolecular hydrogen bonds and aromatic walls formed by the calixarene.

The structure of a self-assembled calixarene aqua-channel system.

The crystal structure of the complex 12.calix-[4]-arene dihydroxyphosphonic acid, 12.propane diammonium, 12.

[Hydroxy(aryl)methylene]diphosphonic acids, a class of drugs in bone pathology treatments, crystallize as head-to-head dimers.

Two [hydroxy(aryl)methylene]diphosphonic acids have been crystallized as dimers. The first compound, [hydroxy(phenyl)methylene]diphosphonic acid monohydrate, C(7)H(10)O(7)P(2).H(2)O, crystallizes in the non-centrosymmetric space group P2(1), with the two enantiomers related by a non-crystallographic centre of inversion, while the second compound, [hydroxy(4-nitrophenyl)methylene]diphosphonic acid tetrahydrofuran disolvate, C(7)H(9)NO(9)P(2).