Significance: Many reports have underscored the importance of the heme degradation
pathway that is regulated by heme oxygenase (HO). This reaction releases bile pigments …

Covering: up to 2006 Heme oxygenase (HO) catalyzes O2-dependent regiospecific
conversion of heme to biliverdin, CO and free Fe (II). The heme group is tightly sandwiched …

The iron-dependent oxidase UndA cleaves one C3–H bond and the C1–C2 bond of
dodecanoic acid to produce 1-undecene and CO2. A published X-ray crystal structure …

Numerous near-infrared (NIR) fluorescent proteins (FPs) were recently engineered from
bacterial photoreceptors but lack of their systematic comparison makes researcher's choice …

Heme oxygenase 1 (HO-1), the rate-limiting enzyme in heme degradation, is involved in the
maintenance of cellular homeostasis, exerting a cytoprotective role by its antioxidative and …

Heme oxygenase (HO), the rate-limiting step in the degradation of heme to biliverdin, ferrous
ion, and carbon monoxide (CO), is an ancestral protective enzyme conserved across …

Horseradish peroxidase (HRP) mediates efficient conversion of many phenolic
contaminants and thus has potential applications for pollution control. Such potentially …

Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal
structures of apo-and heme-bound truncated human HO-2 reveal a primarily α-helical …

The report uses density functional theory to address the mechanism of heme degradation by
the enzyme heme oxygenase (HO) using a model ferric hydroperoxide complex. HO is …

Self-labeling proteins have revolutionized super-resolution and sensor imaging. Tags
recognize a bioorthogonal substrate for covalent attachment. We show the small Ultra-Red …