Coboglobin

Coboglobin is the primary oxygen-carrying biomolecule of the Noelaran. It functions similarly to hemoglobin in Humans but incorporates a central cobalt ion bound within a corrinoid macrocycle resembling an advanced form of vitamin B₁₂.

The high-oxygen, high-carbon-dioxide atmosphere of Nola Prime shaped its evolution, producing a pigment that binds oxygen rapidly but lightly, allowing efficient delivery under extreme biological loads.

Coboglobin

Structure

Coboglobin consists of:

• a single **Co²⁺/Co³⁺ ion**,
• a corrinoid ring similar to cobalamin,
• boron-linked sidechains,
• halogenated ligands stabilizing the oxygen-binding site.

This complex is encapsulated within Noelaran “violet cells,” functionally analogous to red blood cells.

Oxygen Binding

Coboglobin does not form classic oxyhemoglobin. Instead, it stabilizes a **superoxo-like complex**:

Co²⁺ + O₂ ⇌ Co³⁺–O₂⁻

This intermediate is strengthened by nearby borate groups within the protein, enabling:

• rapid oxygen uptake in the lungs,
• strong but reversible binding,
• and efficient release in high-CO₂ tissues.

Biological Role

Coboglobin enables Noelaran physiology by:

• supplying dense musculature with extreme oxygen throughput,
• resisting oxidation from Nola Prime’s 40% O₂ atmosphere,
• functioning efficiently under 1.5 G gravity.

See Also

• Nickoglobin
• Noelaran
• Nola Prime
• Boron Biochemistry
• Pacifism Field