Results 81 to 90 of about 21,602 (293)
Abstract Right ventricular failure (RVF) is a common complication following left ventricular assist device (LVAD) implantation and increases patient morbidity and mortality. Due to the complex and limited understanding of RVF pathophysiology, efforts to prognosticate RVF after LVAD have been challenging.
Abdul‐Fatawu Osman+11 more
wiley +1 more source
Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reducing ...
Thomas Spatzal+3 more
doaj +1 more source
Reactions of ligands 5‐methyl‐N‐(quinolin‐8‐yl)pyrazine‐2‐carboxamide (L1), N‐( N‐(pyridin‐2‐ylmethyl)pyrazine‐2‐carboxamide (L2), N‐(quinolin‐8‐yl)picolinamide (L3), N‐(quinolin‐8‐yl)quinoline‐2‐carboxamide (L4) with the MnCl2.4H2O salt afforded the respective manganese complexes [Mn(L1)(CH3OH)2Cl] (Mn1), [Mn(L2)2] (Mn2) [Mn(L3)2] (Mn3) and [Mn2(L4)2 ...
Nokwanda Tsaulwayo+3 more
wiley +1 more source
A minimalist chemical model of matrix metalloproteinases- Can small peptides mimic the more rigid metal binding sites of proteins? [PDF]
In order to develop a minimalist chemical model of matrix metalloproteinases (MMPs), we synthesized a pentadecapeptide (Ac-KAHEFGHSLGLDHSK-NH2) corresponding to the catalytic zinc(II) binding site of human MMP-13.
Aguilar+48 more
core +1 more source
Towards the spatial resolution of metalloprotein charge states by detailed modeling of XFEL crystallographic diffraction. [PDF]
Oxidation states of individual metal atoms within a metalloprotein can be assigned by examining X-ray absorption edges, which shift to higher energy for progressively more positive valence numbers.
Holton, James M+3 more
core +2 more sources
Electrochemistry of metalloproteins
The direct (unmediated) electrochemistry of a variety of redox proteins has been studied at a range of electrode materials. Electrochemical studies using cytochromes, iron-sulphur proteins and copper proteins show a marked enhancement of the heterogeneous electron-transfer rate at the "edge" plane of pyrolytic graphite. Parallel ESCA studies have shown
Oliver, B, Oliver, B. Nigel
openaire +1 more source
Electron Flow through Metalloproteins [PDF]
Electron transfers in photosynthesis and respiration commonly occur between metal-containing cofactors that are separated by large molecular distances. Understanding the underlying physics and chemistry of these biological electron transfer processes is the goal of much of the work in our laboratories.
Gray, Harry B., Winkler, Jay R.
openaire +8 more sources
Schematic illustration of structural and functional biomimicry. The upper part shows BP with various structures such as monolayered, surface‐microstructural, bilayered and multilayered. The bottom part exhibits BP with different functions including immune regulation, drugs/cells/factors/ions loading, as well as bioelectrical stimulation and ...
Yuhan Du+7 more
wiley +1 more source
Uranyl Binding to Proteins and Structural-Functional Impacts
The widespread use of uranium for civilian purposes causes a worldwide concern of its threat to human health due to the long-lived radioactivity of uranium and the high toxicity of uranyl ion (UO22+).
Ying-Wu Lin
doaj +1 more source
Effect of ELF e.m. fields on metalloprotein redox-active sites [PDF]
The peculiarity of the distribution and geometry of metallic ions in enzymes pushed us to set the hypothesis that metallic ions in active-site act like tiny antennas able to pick up very feeble e.m. signals. Enzymatic activity of Cu2+, Zn2+ Superoxide Dismutase (SOD1) and Fe2+ Xanthine Oxidase (XO) has been studied, following in vitro generation and ...
arxiv