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.