Oxygen activation and radical transformations in heme proteins and metalloporphyrins

X Huang, JT Groves - Chemical reviews, 2017 - ACS Publications
As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply
of metalloproteins for oxidative metabolism and protection against reactive oxygen species …

Lipid oxidation and antioxidant delivery systems in muscle food

H Wu, MP Richards, I Undeland - Comprehensive Reviews in …, 2022 - Wiley Online Library
Lipid oxidation accelerates quality deterioration in muscle‐based foods (fish, red meat, and
poultry), resulting in off‐odors/flavors, color problems, texture defects, and safety concerns …

[PDF][PDF] Polder maps: improving OMIT maps by excluding bulk solvent

D Liebschner, PV Afonine, NW Moriarty… - … Section D: Structural …, 2017 - journals.iucr.org
The crystallographic maps that are routinely used during the structure-solution workflow are
almost always model-biased because model information is used for their calculation. As …

Second sphere effects on oxygen reduction and peroxide activation by mononuclear iron porphyrins and related systems

S Bhunia, A Ghatak, A Dey - Chemical Reviews, 2022 - ACS Publications
Activation and reduction of O2 and H2O2 by synthetic and biosynthetic iron porphyrin
models have proved to be a versatile platform for evaluating second-sphere effects deemed …

[PDF][PDF] Towards automated crystallographic structure refinement with phenix. refine

PV Afonine, RW Grosse-Kunstleve… - … Section D: Biological …, 2012 - journals.iucr.org
phenix. refine is a program within the PHENIX package that supports crystallographic
structure refinement against experimental data with a wide range of upper resolution limits …

The relation between the divergence of sequence and structure in proteins.

C Chothia, AM Lesk - The EMBO journal, 1986 - embopress.org
Homologous proteins have regions which retain the same general fold and regions where
the folds differ. For pairs of distantly related proteins (residue identity approximately 20%) …

Structure and function of haemoglobins

DA Gell - Blood Cells, Molecules, and Diseases, 2018 - Elsevier
Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential
for O 2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a …

Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase‐trimethoprim, a drug‐receptor system

P Dauber‐Osguthorpe, VA Roberts… - Proteins: Structure …, 1988 - Wiley Online Library
A study of the binding of the antibacterial agent trimethoprim to Escherichia coli
dihydrofolate reductase was carried out using energy minimization techniques with both a …

Synthetic Fe/Cu complexes: toward understanding heme-copper oxidase structure and function

SM Adam, GB Wijeratne, PJ Rogler, DE Diaz… - Chemical …, 2018 - ACS Publications
Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

Hydrogen bonding in globular proteins

EN Baker, RE Hubbard - Progress in biophysics and molecular biology, 1984 - Elsevier
1. Main Chain Hydrogen Bondin#(a) Number of hydrogen bonds (b) Saturation of hydroqen
bondinq potential (c) NH. qroups with more than one hydrogen bond (d) C~ O groups with …