Metalloenzymes catalyze a variety of reactions using a limited number of natural amino
acids and metallocofactors. Therefore, the environment beyond the primary coordination …

Many oxidation–reduction (redox) enzymes, particularly oxygenases, have roles in reactions
that make and break C–C bonds. The list includes cytochrome P450 and other heme-based …

The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2),
catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (ie …

Severe hemolysis or myolysis occurring during pathological states, such as sickle cell
disease, ischemia reperfusion, and malaria results in high levels of free heme, causing …

Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the
degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of …

Understanding the processes governing the ability of the heart to repair and regenerate after
injury is crucial for developing translational medical solutions. New avenues of exploration …

The heme-heme oxygenase system has recently been recognized to possess important
regulatory properties. It is tightly involved in both physiological as well as pathophysiological …

We review gases that can affect oxidative stress and that themselves may be radicals. We
discuss O2 toxicity, invoking superoxide, hydrogen peroxide, and the hydroxyl radical. We …

Hemopexin is an acute-phase plasma glycoprotein, produced mainly by the liver and
released into plasma, where it binds heme with high affinity. Other sites of hemopexin …

Carbon monoxide is now well-established as a small-molecule biological effector in the
human body. Metal–carbonyl complexes are a promising way to achieve safe and controlled …