Rubrerythrin

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PDB 1nnq EBI

Rubrerythrin is a non-heme iron protein that plays a crucial role in the oxidative stress response in anaerobic and microaerophilic bacteria. It is characterized by its unique structure, which includes iron-binding sites that are essential for its function in reducing hydrogen peroxide to water, thereby protecting cells from oxidative damage.

Structure

Rubrerythrin is composed of two iron centers: a diiron site and a rubredoxin-like FeCys4 site. The diiron site is responsible for the reduction of hydrogen peroxide, while the rubredoxin-like site is involved in electron transfer processes. The protein typically forms a homodimer, with each monomer contributing to the overall function of the enzyme.

Function

The primary function of rubrerythrin is to detoxify reactive oxygen species (ROS), particularly hydrogen peroxide. This activity is crucial for the survival of anaerobic and microaerophilic organisms, which are often exposed to oxidative stress. Rubrerythrin reduces hydrogen peroxide to water, thereby mitigating the potential damage caused by ROS.

Biological Significance

Rubrerythrin is found in a variety of anaerobic and microaerophilic bacteria, including species of the genera Clostridium, Desulfovibrio, and Bacteroides. Its presence is often associated with environments where oxidative stress is a significant challenge, such as in the human gut or in anaerobic sediments.

Related Proteins

Rubrerythrin is part of a larger family of non-heme iron proteins that include rubredoxin, desulfoferrodoxin, and superoxide reductase. These proteins share similar functions in protecting cells from oxidative damage but differ in their specific mechanisms and structures.

Research and Applications

Research on rubrerythrin has provided insights into the mechanisms of oxidative stress resistance in anaerobic organisms. Understanding these mechanisms can have applications in biotechnology, such as the development of stress-resistant microbial strains for industrial processes.

See Also

• Rubredoxin
• Desulfoferrodoxin
• Superoxide reductase
• Oxidative stress
• Anaerobic bacteria