Hemoglobiinissa

Hemoglobiinissa is a hypothetical globin-like protein used in educational contexts and fictional biology to illustrate principles of oxygen transport and protein allostery. The name blends hemoglobin with the -issa suffix, signaling its status as a modeled member of the globin family.

Its proposed structure is tetrameric, composed of two alpha-like and two beta-like subunits. Each subunit contains a heme prosthetic group with ferrous iron capable of reversible oxygen binding. Subunit interactions produce cooperativity, yielding a sigmoidal oxygen-binding curve. In theoretical variants, binding affinity can be modulated by allosteric effectors that simulate changes in the intracellular environment, illustrating how factors such as pH or ionic strength influence oxygen affinity.

Physiologically, in educational scenarios, hemoglobiinissa transports oxygen from respiratory sites to tissues, releasing O2 as pO2 decreases or pH falls. It can also model interactions with other ligands, such as carbon monoxide or nitric oxide, to discuss competing binding and affinity shifts in a controlled context. The concept serves to demonstrate physiological trade-offs without referring to an actual organism.

Genetics in the model are simplified to a hypothetical gene family Hgb-issa encoding four globin-like genes corresponding to the four subunits; expression patterns are presented as developmental or tissue-specific in simulations. Evolutionary discussions use hemoglobiinissa to illustrate gene duplication and divergence within globin families.

See also: Hemoglobin, Myoglobin, Globin family, Heme.